Peptides

HLA-A*02 is a class I major histocompatibility complex (MHC) allele which is part of the HLA-A group of human major histocompatibility complex (MHC) leukocyte antigens (HLA). HLA-A is a human MHC class I cell surface receptor and is involved in presenting short polypeptides to the immune system. These polypeptides are typically 7-11 amino acids in length and originate from proteins being expressed by the cell. Cytotoxic T cells in the blood "read" the peptide presented by the complex and should only bind to non-self peptides. If binding occurs, a series of events is initiated culminating in cell death via apoptosis. Melanoma-associated antigen 1 (MAGE-A1) is part of a well-characterized group of cancer/testis antigens (CTA) that are encoded as a separate cluster on the X chromosome. MAGE-I antigens are mainly expressed in highly proliferating cells, such as cancer cells and therefore may be ideal targets for cancer immunotherapy. Expression of MAGEs has been reported several types of cancer including: lung- breast- thyroid- colon- stomach- liver and bladder where MAGE-A is considered to be a poor prognostic factor.This peptide corresponds to part of the MAGE-A1 sequence which is presented on the MHC class I antigen HLA-A*02.

Histone H3.3 is a replication-independent histone variant, which replaces canonical histone H3.1/2 outside of S phase. H3.3 is expressed throughout the cell cycle, as well as in quiescent cells and is referred to as the 'replacement histone'. H3.3 is largely deposited in a DNA synthesis-independent fashion by a distinct set of chaperones proteins. H3.3 accumulates in post mitotic cells, such as cerebral cortical neurons and is incorporated at sites of UV damage where it protects against sensitivity to UV light. H3.3 deposition occurs on DNA sequences that are transiently nucleosome-free, such as during transcription and DNA repair, therefore serving as a marker for regions of high transcriptional activity. H3.3 is also enriched in heterochromatic subtelomeric and pericentromeric regions. H3.3 plays important roles in many developmental contexts such as in stem cells, during fertilization and reproduction and during reprogramming of genomes following fertilization or somatic cell nuclear transfer. Mutations in histone H3.3 are common events in certain cancers.

This peptide is recognised and cleaved by the enzyme Sortase A (SrtA) from-Staphylococcus aureus. The catalytic cysteine residue in the active site of SrtA serves as a nucleophile to cleave the peptide bond between threonine and glycine. Cleavage results in the formation of a thioacyl intermediate between the peptide and SrtA. This intermediate is then resolved by the N-terminus of an (oligo)glycine nucleophile, resulting in the creation of a new peptide bond that links the peptide and its biotin tag to the incoming nucleophile.- This method of protein labelling is known as sortagging.This peptide contains an N-terminal biotin tag for detection and purification.

Histone deacetylases (HDACs) are a family of enzymes which are highly evolutionary conserved across all eukaryotes. HDACs modify histones by removing acetyl groups from the tail regions. Histone deacetylation is generally associated with reduced gene expression due to a more compact chromatin state less accessibility for transcription factors (TFs). HDACs are essential for many physiological processes including development and cellular homeostasis. They also play an important role in disease states, including neurodegenerative disorders, genetic diseases and cancers.This peptide is the fluorogenic substrate for assaying histone deacetylase (HDAC) activity in a two-step enzymatic reaction. The assay consists of the initial lysine deacetylation by HDAC followed by the release of the fluorescent group by trypsin. Fluorescence can be detected upon fluorophore release.

Peptide derived from the Gastric inhibitory polypeptide (GIP), an inhibiting hormone of the secretin family of hormones. While GIP is a weak inhibitor of gastric acid secretion, its main role is to stimulate insulin secretion - in a glucose-dependent mechanism. Therefore, GIP is referred to as a glucose-dependent insulinotropic peptide.GIP is derived from a 153-amino acid pro-protein encoded by the GIP gene and circulates as a biologically active 42-amino acid peptide. It is synthesised by K cells, which are found in the mucosa of the duodenum and the jejunum of the gastrointestinal tract. GIP receptors are seven-transmembrane proteins found on β-cells in the pancreas. These β-cells are those that are able to simultaneously detect glucose and release insulin as a result to GIP binding.The clinical relevance of GIP is related to type 2 diabetes mellitus (T2DM)- studies have found that T2DM diabetics are unresponsive to GIP and have lower levels of GIP secretion after a meal when compared to non-diabetics. In research involving knockout mice, it was found that absence of the GIP receptors correlates with resistance to obesity.

Peptide derived from GP33, an epitope of the lymphocytic choriomeningitis virus (LCMV) which produces a CD8+ cytotoxic T lymphocyte response.

The SARS-CoV-2 non-structural protein 13 (NSP13) has been identified as a target for anti-viral therapeutics due to its highly conserved sequence and is essential for viral replication.  NSP13 is part of the helicase superfamily 1B. As an NTPase and RNA helicase, NSP13 binds to RNA-dependent RNA polymerase and acts in concert with the replication-transcription complex to stimulate backtracking and further activate NSP13 helicase activity. These factors make NSP13 a good target for developing new antiviral drugs. In addition, the identification of epitopes within the NSP13 sequence can help design more effective SARS-CoV-2 vaccines.Models have predicted epitopes exhibiting antigenicity, stability and interactions with MHC class-I and class-II molecules. NSP13 (426-440) is an epitope candidate with various HLA restrictions. This epitope can be used to better vaccine design for more durable CD4+ and CD8+ T cell responses for long-lasting immunity.

This peptide is phosphorylated by Janus kinase 1 (JAK1) and is an ideal substrate for use in kinase assays. The JAK family of kinases is essential for the signalling of a host of immune modulators in tumour, stromal, and immune cells where they are highly expressed. JAK family proteins mediate the signalling of the interferon (IFN), IL-6, and IL-2 families of cytokines.JAK kinases are associated with cytokine receptors. Cytokine binding to these receptors results in activation of JAK kinases and receptor phosphorylation. Phosphorylated cytokine receptors recruit STAT proteins, which are then phosphorylated by the activated JAK kinases. Phosphorylated STAT proteins form homo- and hetero-dimers that translocate into the nucleus and function as transcription factors.This JAK1 substrate peptide contains an N-terminal Biotin and a phospho-tyrosine residue

The Dystrophin protein, encoded by the dystrophin gene, is part of the dystrophin glycoprotein complex which connects the inner cytoskeleton to the extracellular matrix in muscle fibres. This allows the muscle cell plasma membrane to remain structurally stable.Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive and cause the gradually weakening of the muscles leading to respiratory failure and ultimately reduces the patient lifespan.In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.

Amyloid β-peptide (Aβ) has been identified as the key subunit of the extracellular plaques found in the brains of patients with Alzheimer's disease (AD) and Down's syndrome (DS). Aβ has therefore been extensively studied as a potential target for treatment of AD.Aβ is formed from the cleavage of the large, transmembrane protein- APP (amyloid precursor protein). Cleavage of APP by β- and then γ-secretases results in the formation of Aβ. Aβ can aggregate to produce amyloid-β oligomers, which are thought to be highly neurotoxic. Over time Aβ can further aggregate to produce the characteristic senile plaques present in AD and DS.Aβ can be degraded by enzymes such as neprilysin, insulin degrading enzyme or endothelin converting enzyme. At physiological levels Aβ may be involved in controlling synaptic activity and neuronal survival.Aβ1-40 is a major C terminal variant of amyloid β constituting the most abundant AB peptide in the human brain.

Ovalbumin (OVA) is the primary protein in egg-white, and is involved in initiating food allergies and asthma. It is a highly immunogenic protein and can be used for peptide conjugation in the development of antibodies.OVA (324-340) is a class I (Kb)-restricted peptide epitope of OVA. The ovalbumin fragment is presented by the class I MHC molecule, H-2Kb.

ACE I is a peptidyl-dipeptidase that has been well studied due to its crucial role in blood pressure regulation- ACE I converts angiotensin II to angiotensin I plus degradation of bradykinin as part of the circulating renin-angiotensin system (RAS). ACE I is involved in age-related neurodegeneration. Deregulation of dopamine is evident in Alzheimer's disease and Parkinson's disease with links to RAS. Acein has been shown to interact with ACE I with high affinity without effecting peptidase activity. Furthermore, acein was shown to stimulate dopamine release from rat brain tissue in vitro and in vivo. The mechanism of action has yet to be uncovered.

The ionic-complementary octapeptide, FEFEFKFK, can self-assemble into antiparallel β-sheet rich fibres and forms very stable hydrogels when at a concentration of more than 20 mg/mL (in water).These peptide hydrogels are naturally biocompatible and biodegradable and can be metabolised by the body. Such hydrogels have been shown to mimic the structure of the extracellular matrix, thus offering cells a niche to undertake their physiological functions. These properties mean that these hydrogels have the potential for use in medical applications.FEFEFKFK hydrogels are able to support the culture of cells such as mesenchymal stem cells in three dimensions with sustained cell viability. They can also support the differentiation into osteoblasts and promote mineralisation upon addition of osteogenic stimulation. They therefore have potential for use in the regeneration of hard tissues such as alveolar bone following injury or degeneration.

CREB327/active transcription factor CREB-A (113-126), human.

Cyclic L27-11 is a peptidomimetic compound that targets the outer membrane protein LptD. LptD is part of a complex that functions to transport lipopolysaccharides to the cell surface through the C-terminal β-barrel domain lumen, embedded within the outer membrane. Cyclic L27-11 can bind LptD and prevent translocation of lipopolysaccharides across the periplasm, even nanomolar doses were effective. This interaction gives cyclic L27-11 a potent antimicrobial activity particularly against the human pathogen Pseudomonas aeruginosa.Modifications of cyclic L27-11 are under research to improve its stability for drug delivery. The peptide provided here has a D-proline substitution, characterised as have no antimicrobial activity against Pseudomonas aeruginosa.

Histone H3 (32-47) is derived from Histone 3 (H3) which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into a structure known as the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. Both H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Similar to the other core histone, H3 has a globular domain and a flexible N-terminal domain, 'histone tail' which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter the positioning of the nucleosome, allowing the DNA it to be either available or inaccessible to the transcription machinery.

Ac-Arg-Leu-Arg-MCA is a fluorogenic substrate for the proteasome that can be used in proteasome research. Ac-Arg-Leu-Arg-MCA has been shown to be a useful fluorescent substrate for the ubiquitin proteasome system substrates and peptides and biochemicals. It is also an Enzyme Substrate of the Peptides & Biochemicals section.

Myelin oligodendrocyte glycoprotein (MOG) is a member of the immunoglobulin (Ig) protein superfamily and is expressed exclusively in the central nervous system (CNS) on the surface of myelin sheaths and oligodendrocyte processes. MOG is expressed at the onset of myelination, and therefore is a potential marker for oligodendrocyte maturation.MOG contains an extracellular domain, a transmembrane domain, a cytoplasmic loop, a membrane-associated region and a cytoplasmic tail.  MOG may function as a cell surface receptor or cell adhesion molecule.  Fifteen different alternatively spliced isoforms have been detected in humans. These are present either on the cell surface, the endoplasmic reticulum in the endocytic system, or in secreted form.The secreted form of MOG may trigger autoimmunity if released into the cerebrospinal fluid and periphery. MOG is thought to be a key target for auto-antibodies and cell-mediated immune responses in inflammatory demyelinating diseases such as multiple sclerosis (MS) and is therefore widely studied in this field.The MOG (35-55) fragment is the most potent auto-antigenic region of MOG, and the most effective at inducing experimental autoimmune/allergic encephalomyelitis (EAE), an animal model that resembles MS. This peptide has an uncharged C-terminal amide, an acid form is also available in our catalogue.

TP10 is an amphipathic cell-penetrating peptide (CPPs) known as transportan 10. Its formation involves the use of a lysine residue to form a chimeric linkage between a mastoparan 21-residue peptide, a wasp venon 14-residue peptide and 6-residues derived from the neuropeptide galanin. Structurally TP10 contains only positively charged amino acids along with 4 lysines and an N-terminus. Therefore it will produce a +5 charge under conditions of a neutral pH. It has been found that TP10 may aid molecules in penetrating through the cell membrane barrier through directly interacting with the lipid bilayer. During these interactions with the membrane TP10 will form an amphipathic α-helix. Consequently TP10 can be used in transduction methods.It contains 5-Carboxyfluorescein (5-FAM), a widely used green fluorescent tag.

Histone H3 (1-20)-GG-[Lys(5-FAM)] is derived from Histone 3 (H3) which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. Both H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Similar to the other core histone, H3 has a globular domain and a flexible N-terminal domain, 'histone tail' which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter the positioning of the nucleosome, allowing the DNA it to be either available or inaccessible to the transcription machinery.Histone H3 (1-20)-GG-[Lys(5-FAM)] has a C-terminal GKK linker labelled with 5-Carboxyfluorescein (5-FAM), a widely used green fluorescent tag. This peptide also has an uncharged C-terminal amide.

The pathology of cardiovascular disease (CVD) is linked to the health of endothelial cells in the heart.- However, the specific characteristics of the cardiovascular endothelial cells are still being uncovered. The heart homing peptide specifically binds to a receptor on cardiovascular endothelial cells. This peptide can be used as a conjugate to deliver molecules specifically to the heart. This can be a crucial tool in therapeutic drug delivery for CVD, angiogenesis, and thrombosis.

α-connexin carboxyl terminal peptide that specifically targets and maintains Cx43 at gap junction sites between cell-cell membrane borders of breast cancer cell.- Thus it augments gap junction activity and impairs proliferation and survival of breast cancer cells with no effect on non-transformed cells.

Histone H3 (1-20) K4Me3-GG-[Lys(5-FAM)] is derived from Histone 3 (H3) which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. Both H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Similar to the other core histone, H3 has a globular domain and a flexible N-terminal domain, 'histone tail' which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter the positioning of the nucleosome, allowing the DNA it to be either available or inaccessible to the transcription machinery.The lysine at position 4 of this peptide has been tri-methylated and it is implicated in studies that this modification may remodel the chromatin so that it is more accessible to transcription factors, which may ultimately increase the level of gene expression.Additionally, Histone H3 (1-20) K4Me3-GG-[Lys(5-FAM)] has a C-terminal GKK linker labelled with 5-Carboxyfluorescein (5-FAM), a widely used green fluorescent tag. This peptide also has an uncharged C-terminal amide.

Diprotin B is a colony-stimulating factor protein that has inhibitory properties in the colon. It has been shown to be effective in reducing symptoms of bowel disease and inflammatory bowel disease, as well as reducing the recurrence of colon cancer. Diprotin B inhibits the release of inflammatory cytokines such as tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6). The inhibition of these proinflammatory cytokines may contribute to the anti-inflammatory effects observed with Diprotin B treatment. Diprotin B also prevents cytosolic calcium accumulation, which can lead to cell lysis. This process is mediated by antimicrobial peptides called defensins that are expressed in Paneth cells found in the small intestine and colon. Defensins have also been shown to induce cell lysis through their ability to bind to bacterial membranes.

Delivery of peptide nucleic acid (PNA) oligonucleotides to targeted cells is becoming a viable therapeutic strategy by redirecting RNA splicing for conditions like Duchenne muscular dystrophy (DMD). The use of novel cell-penetrating peptides (CPP) has helped create targeted, and increased activity of the PNAs delivered.PNA internalization peptides (Pip)  is a specifically designed CPP for conjugation to PNAs. Pips were designed to improve PNA activity observed in HeLa cells determined by splicing redirection assays and increased serum stability determined by mass spectrometry. Of the Pip series, Pip1 enters the cell in an energy-dependent manner, primarily via clathrin-dependent endocytosis. Pip1 conjugated to a PNA was determined to be well transported into the cell but is not the most stable against proteolysis. However, this may benefit some cargo depending on the intracellular destination. As a CPP for DMD, the proteolysis of Pip1 was deemed an issue but showed promise for other conjugates in HeLa cells.Pip1 is labelled at the N-terminus with an alkyne attachment for ease of reaction with an opposite Click reactive partner (azide). Azide-alkyne cycloaddition has become the most popular Click reaction. Alkyne-Pip1 allows various applications, particularly for protein conjugation, modification, and drug delivery.

Aminopeptidase fluorogenic substrate. Upon cleavage of the bond between leucine and the 7-amino-4-trifluoromethylcoumarin (AFC) group an increase in fluorescence between 495-505nm can be detected using an excitation wavelength of 395-400nm.

Boc-D-Ile-OH is a cyclohexanone that can be used in peptide synthesis. It has been shown to have affinity for the Tools for Peptide Synthesis and is able to activate primary tumors with metastasis. Boc-D-Ile-OH has been shown to have kinetic parameters, and its pharmacophores are characterized by an organic chemistry approach. This compound is a serine protease inhibitor that blocks the activity of other serine proteases such as chymotrypsin and trypsin.

Protease activated receptors (PARs) are a distinctive four-member family of seven transmembrane G protein-coupled receptors (GPCRs) widely expressed in inflammatory cells. PARs are cleaved by certain serine proteases to expose a tethered ligand domain, this ligand domain then binds to and activates the receptors to initiate multiple signalling cascades. These PAR-activating proteases therefore represent PAR agonists. This PAR-4 agonist peptide represents the N-terminal sequence of the 'tethered ligand' and is therefore capable of activating the receptor independently of N-terminal proteolysis.

Human adrenocorticotropic hormone (ACTH) also known as corticotropin. ACTH is a tropic hormone produced and secreted by the anterior pituitary gland and member of the melanocortins peptide family. ACTH is cleaved from the precursor proopiomelanocortin (POMC). ACTH is an important component of the hypothalamic-pituitary-adrenal (HPA) axis and is often produced in response to biological stress. ACTH acts to increase the production and release of cortisol via its interaction with the ACTH receptor ACTHR, also known as melanocortin type 2 receptor (MC2R). Receptor activation increases the intracellular concentration of cAMP via adenylyl cyclase.Abnormal ACTH levels in the body has been linked to primary adrenal insufficiency/Addison's disease, Cushing's disease and secondary adrenal insufficiency

Histone H3 (1-18) is derived from Histone 3 (H3) which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. Both H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Similar to the other core histone, H3 has a globular domain and a flexible N-terminal domain 'histone tail' which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter the positioning of the nucleosome, allowing the DNA it to be either available or inaccessible to the transcription machinery.

C5a receptor peptide antagonist which can ameliorate experimentally-induced colon inflammation in mice. It can also reduce fibrillar amyloid deposits, decrease hyperphosphorylated tau levels and rescue cognitive function in a mouse model of Alzheimer's Disease. Also improves hindlimb grip strength and slows disease progression in the hSOD1G93A-mouse model of amyotrophic lateral sclerosis. Orally active and brain penetrant.

Amyloid β 1-15 (Aβ1-15) is one of many short Aβ species found in vivo and is formed by the cleavage of amyloid β precursor protein by β- and alpha-secretase.Aβ has been identified as the key subunit of the extracellular plaques found in the brains of patients with Alzheimer's disease (AD) and Down's syndrome (DS). Aβ has therefore been extensively studied as a potential target for treatment of AD.Aβ is formed from the cleavage of the large, transmembrane protein- APP (amyloid precursor protein). Cleavage of APP by β- and then γ-secretases results in the formation of Aβ. Aβ can aggregate to produce amyloid-β oligomers, which are thought to be highly neurotoxic. Over time Aβ can further aggregate to produce the characteristic senile plaques present in AD and DS. Aβ can be degraded by enzymes such as neprilysin, insulin degrading enzyme or endothelin converting enzyme. At physiological levels Aβ may be involved in controlling synaptic activity and neuronal survival.Contains an N-terminal Carboxytetramethylrhodamine (TAMRA) fluorophore. TAMRA is a pH-stable orange-red fluorescenct dye with good photostability.

Human Papillomavirus (HPV) E7 protein (49-57) immunogenic Human Cytotoxic T lymphocytes (CTL) epitope encoded by human papillomavirus 16 type E7 with very high affinity binding to defined HLA molecule. CEF control peptides are the gold standard for effectively stimulating adaptive immune cells in cytokine assays.

The pathology of coronary heart disease (CHD) and ischemia are linked to the health of endothelial cells in the heart.- However, providing molecular therapies specifically into myocardium remains elusive. The cardiac targeting peptide (CTP) was shown to specifically transduce cardiomyocytes as it is a cationic PTD.This peptide can be used as a conjugate to deliver molecules specifically to the heart. This can be a crucial tool for research into therapeutic drug delivery for ischemic attacks and infarctions. This peptide is research quality and therefore for research purposes only, and not for use in a therapeutic setting.

Mammalian bombesin-like peptide neurotransmitter that is an agonist for the gastrin-releasing peptide receptor (GRPR). It exhibits physiological functions such as gastrin and somatostatin release and chemoattraction within the immune system.

IL-33 is a member of the IL-1 superfamily of cytokines, a determination based in part on the molecules β-trefoil structure, a conserved structure type described in other IL-1 cytokines. IL-33 acts intracellularly as a nuclear factor and extracellularly as a cytokine.IL-33 has been associated with several disease states through Genome Wide Association Studies: asthma, allergy, endometriosis and hay fever. A single-nucleotide polymorphism rs928413 (A/G), is located in the 5' upstream region of IL33 gene, and its minor 'G' allele was identified as a susceptible variant for early childhood asthma and atopic asthma development.

Immunogenic Human Cytotoxic T lymphocytes (CTL) epitope encoded by human papillomavirus 16 type E7 with very high affinity binding to the HLA-A*0201 molecule.

Portion of HCMV pp65

Custom research peptide; min purity 95%. For different specs please use the Peptide Quote Tool

Neuropeptide S (NPS) is a neuropeptide found in mammalian brains, primarily in neurons in the lateral parabrachial nucleus, the-peri-locus coeruleus and the principle sensory 5 nucleus of the trigeminus. NPS is involved in several neuroendocrine, behavioural and inflammatory responses, including: reducing anxiety in mice- suppressing appetite and inducing wakefulness and hyperactivity. NPS treatment can be used to improve fear extinction in mice and limit fear memory retrieval after fear reduction training, thus making it an interesting target for treatment of post-traumatic stress disorder. NPS exerts its actions by binding to a G-protein coupled receptor, NPSR

Vasoactive intestinal peptide (VIP) is a neuropeptide found throughout the body and the central nervous system (CNS). VIP is located within cell bodies and nerve endings of the enteric nervous system, brain and pancreas. VIP neurons in the peripheral system fire to regulate blood vessels, and the  CNS innervate cerebral vasculature. VIP  binds to G protein-coupled receptors VPAC1 and VPAC2. VIP and VPAC2 are detected in circular smooth muscle cells of cerebral arterioles. VIP and VPAC1 are also found in lymphatic tissue. VIP can block inflammation, modify the Th response favouring Th2 and induce regulatory T cells. VIP has been recognised as an immunosuppressive neuropeptide and studied as a treatment for inflammatory conditions. Model administration of VIP and VIP (1-12) can reduce the severity of experimental autoimmune encephalomyelitis (EAE). This suggests VIP and fragment (1-12) could lead to VIP-based therapies for inflammatory disorders such as multiple sclerosis (MS).The VIP N-terminal (1-12) has also been used in mass spectrometry as a control and to generate a method for C-terminal sequence analysis by MALDI-TOF MS.

Portion of EBV

The cleavage of proglucagon forms glucagon. Increased levels of glucagon that can't be regulated are linked to diabetic hyperglycaemia and other pathologies. Typically, glucagon levels should be suppressed as glucose levels rise. However, the opposite has generally been found to be accurate, and the nature of this elevated immunoreactive glucagon has led to more research. Hyperglucagonaemia is a characteristic of several pathologies, but the detection of immunoreactive glucagon has yet to be fully verified due to the nature of available detection.Glucagon can be hydrolysed by dipeptidyl peptidase IV (DPIV) to products such as (18-29) and (3-29). Current methods for detecting glucagon rely on antibodies to the N terminus or  C-terminus to detect pancreatic glucagon. However, these antibodies may also detect truncated forms due to a pathology affecting the secretion, clearance or processing of proglucagon-derived peptides. Theoretically, these can be used in a sandwich process to detect only full-length glucagon. Therefore, the availability of the truncated glucagon (3-29) as a control to test the sensitivity of the available antibodies and the ELISAs is useful. Plasma levels from hyperglucagonaemic patients and healthy counterparts were used as a control to test the commercial glucagon assays and ELISAs. The truncated glucagon (3-29) provided valuable information about the sensitivity and specificity of the antibodies that have been used as an industry standard for glucagon measurement. This truncated glucagon is vital in ensuring our research moves forward with more controls and fewer assumptions.

NanoLuc (Nluc) is an engineered luciferase protein which was developed from the luciferase of deep-sea shrimp (Oplophorus gracilirostris). This luciferase protein is considerably smaller than firefly or Renilla luciferase yet has higher luminescent intensity.In the NanoBiT assay system the NanoLuc luciferase protein has been separated into a large fragment, LgBiT, and a small fragment SmBiT which corresponds to the C-terminal. When these two fragments interact NanoLuc activity is restored.

CBL (167-180) is derived from the CBL E3 ubiquitin ligase which targets receptor tyrosine kinases to lysosome degradation. CBL and its family member CBL-B are expressed in hematopoietic cells and as E3 ubiquitin ligases they contain a tyrosine kinase domain and an RF domain joined by a linker domain. The function of the RF domain is to transfer ubiquitin from E2 ubiquitin-conjugating enzymes onto the target protein which is often phosphorylated. Consequently the ubiquitinated substrate, the receptor tyrosine kinases, are ultimately targeted to the lysosome for degradation.EGFR is an example of a receptor tyrosine kinase whose activation is prevented by CBL and CBL-B when they bind and recruit GRb2, the adapter protein to EGFR. Consequently the ubiquitinylation of EGFR occurs and targets it for recognition by the endosomal protein complex and then lysosome degradation.It has also been found that the CBL family can negatively regulate through ubiquitinylation, PI 3-kinases, Rap G-protein guanine nucleotide exchange factor (GEF), C3G and Rho GTPase GEF Vav which are all non-receptors.If CBL becomes non-functional it can be associated with malignancies such as acute myeloid leukemia and myelodysplastic syndrome.

Relaxin-3 is part of the insulin/relaxin superfamily with various roles, including appetite, stress, and addiction. Relaxin-3 binds to its cognate receptor relaxin family peptide 3 receptor (RXFP3). B1-22R  is a single-chain relaxin-3 antagonist for RXFP3 no interaction is found with RXFP1 or RXFP4. B1-22R  is a truncation of the B-chain of relaxin-3 and the addition of an arginine residue at the C-terminus-B1-22R acts as a RXFP3 antagonist. B1-22R has been used to perform structural analysis relationships (SARs) and residue scanning to understand the critical residues and conformation of the interaction between B1-22R and RXFP3. B1-22R can generate more potent analogs of relaxin-3 that are more stable and serve as models for drug design targeting the relaxin-3 receptor for regulation of addiction, stress, and appetite.B1-22R is provided in the amide form.

Peptide Ac-KKARFSRFAGSSPSQSSMVAR-NH2 is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice.

Syntide-2 is a substrate peptide which was specifically designed to be homologous to site 2 in glycogen synthase. Syntide-2 is therefore phosphorylated by Ca2+ calmodulin-dependent protein kinase II as well as other calcium dependant kinases and protein kinase C. Synthase-2 can also be phosphorylated by CAMP-dependent protein kinase and to a lesser extent- phosphorylase kinase, but not by myosin light chain kinase.

SARS-CoV-2 Membrane protein (172-188)

Binds to human transferrin receptor (TfR). This 12-amino acid peptide does not compete with transferrin for receptor binding and is able to internalise into TfR expressing cells.

SAMS peptide was originally designed as a selective substrate for mammalian 5' adenosine monophosphate-activated protein kinase (AMPK) for use in kinase assays. However it is also able to be phosphorylated by the yeast AMP homologue- sucrose non-fermenting 1 kinase (SNF1) and SNF1-related kinases (SnRK1) in plants.The conserved family of kinases containing SnRK1, SNF1 and AMPK plays an important role in regulating cellular energy homeostasis.

The histone H2A residues 1-20 are derived from histone 2A (H2A) which is one of the four core his-tones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into a structure known as the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core.At the site of DNA entry on the outer nucleosome, the C-terminus of H2A is present and is able to interact with linker histones or other factors. This allows for variation and changes in nucleosome stability to occur. Furthermore Histone H2A has histone variants such as H2A.Z and H2A.X (which are present in all organisms) and these variants alter the organisation of the DNA.Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter to change the positioning of the nucleosome, allowing the DNA it to be either available to the transcription machinery or inaccessible.

Neurotensin (NT) is involved in food absorption in the gut as well as acting as a neurotransmitter in the central nervous system (CNS). In the intestine, NT increases fatty acid translocation, in part by increasing intestinal blood flow. In the CNS, NT regulates pathways associated with ghrelin and leptin which mediate satiety and food ingestion. NT is also involved in the regulation of Luteinizing hormone (LH) and Prolactin release and also plays a role in hypotension- analgesia- gut contraction- vascular permeability- maintaining energy homeostasis- fat storage and metabolic disorders. Higher plasma pro-NT levels are associated with obesity and insulin resistance. NT is therefore a potential target for treating obesity-related diseases.NT is secreted from neuroendocrine cells in the small intestine upon fat intake and exerts its physiological actions by binding three NT receptor (NTR) types- NTR1, NTR2, and NTR3.NTR1 is highly expressed in various tumour cells including- small cell carcinoma/small cell lung cancer (SCLC)- meningiomas- astrocytomas- glioblastoma- pancreatic and colonic carcinoma, and breast and prostate cancers. NTR1 is therefore a possible target for novel cancer therapy.

Custom research peptide; min purity 95%. For different specs please use the Peptide Quote Tool

HLA-A*02 is a class I major histocompatibility complex (MHC) allele which is part of the HLA-A group of human major histocompatibility complex (MHC) leukocyte antigens (HLA). HLA-A is a human MHC class I cell surface receptor and is involved in presenting short polypeptides to the immune system. These polypeptides are typically 7-11 amino acids in length and originate from proteins being expressed by the cell. Cytotoxic T cells in the blood "read" the peptide presented by the complex and should only bind to non-self peptides. If binding occurs, a series of events is initiated culminating in cell death via apoptosis. New York oesophageal squamous cell carcinoma 1 (NY-ESO-1) is part of a well-characterized group of cancer/testis antigens (CTAs). Normally, NY-ESO-1 expression is restricted to germ cells and placental cells, however NY-ESO-1 is also expressed in several cancers including: neuroblastoma- myeloma- metastatic melanoma- synovial sarcoma as well as bladder- oesophageal- hepatocellular- head and neck- non-small cell lung- ovarian- prostate and breast cancers and is often associated with poor prognosis. NY-ESO-1 is also able to elicit a spontaneous immune response, being the most immunogenic among the CTA family members and is therefore the most promising CTA candidate target for cancer immunotherapy.NY-ESO-1 is coexpressed with melanoma antigen gene C1, a member of the MAGE family of CTAs which is involved in cell cycle progression and apoptosis.

Gene therapy is potentially an ideal treatment for muscle tissue myopathies but targeting remains an issue. The large volume of muscle in the body versus the requirement for tissue-specificity is of particular concern. This heptapeptide has been shown to preferentially bind skeletal myofibers and thus can be used to study targeting of peptide/gene-delivery to muscle tissue. Research into gene therapy of Duchenne muscular dystrophy (DMD) and spinal muscular atrophy (SMA) has been of particular interest with muscle targeting peptides. This product already shows ideal placement to continue that research to overcome some of these issues.

Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2) and its negative regulator Kelch-Like ECH-Associated Protein 1 (Keap1) provide vital protection in maintaining cellular redox. In parallel, Nrf2 also aids the resolution of inflammation and also tissue repair. In homeostatic conditions, the transcription factor Nrf2 is controlled in a cytoplasmic complex with Keap1 with ubiquitination and protein degradation. Nrf2 has been linked to numerous cancers due to mutations affecting the binding region of Nrf2 to Keap1, resulting in Nrf2 dissociating from the complex. Nrf2 constitutively accumulates in the nucleus and activation of prosurvival genes that promote cancer cell proliferation.The Neh2 region of Nrf2 interacts with Keap1, as shown by nuclear magnetic resonance spectroscopy. The 16 amino acid peptide (AFFAQLQLDEETGEFL) (69-84) flanks the conserved ETGE motif and can replicate the binding to keap1.Therapeutics targeting the Nrf2 signalling pathway and activation of Nrf2 is a keen area of research, with many cancers being linked to Nrf2, particularly pancreatic cancer. Additionally, activation of Nrf2 has become a possible target as a treatment for COVID. Nrf2 (69-84) replicating full-length Nrf2 binding has been helpful in all cases. This Nrf2 (69-84) contains a covalently bonded N-terminal Biotin tag that can be used for detection and purification. If you would prefer the simple peptide, Nrf2 (69-84), it is available from our catalogue.

C-type natriuretic peptide (CNP) is a novel urinary biomarker which is part of the natriuretic peptide family. CNP is produced in the kidney and the endothelium and has been localised to renal tubules. CNP expression has also been detected in cardiomyocytes, vascular endothelium, and bone.CNP is synthesized as the precursor 103 amino acid (AA) protein, proCNP (AA 1-103), which is then cleaved into NT-proCNP (AA 1-50) and CNP53 (AA 51-103) by the intracellular endoprotease furin. CNP53 is then cleaved to give the biologically active mature form CNP22 (AA 82-103) and inactive form NT-CNP53 (51-81). CNP primarily acts as an autocrine or paracrine factor and has anti-proliferative and anti-fibrotic properties, including suppression of fibroblast proliferation and collagen production, inhibition of vascular smooth muscle cell proliferation and accelerated regeneration of endothelial cells. CNP is a vasodilator and potent venodilator and slightly elevated levels have been detected in heart failure and renal disease states. CNP has renoprotective properties and is activated during renal injury, where it helps preserve glomerular function and suppress pro-fibrotic processes. Hypoxia, cytokines and fibrotic growth factors, are stimuli for CNP production and release.CNP selectively activates the cell surface particulate guanylyl cyclase receptor B (GC-B), catalysing the conversion of GTP to the downstream second messenger, cyclic guanosine monophosphate (cGMP).

C5a receptor 2 (C5aR2, or C5L2) is a seven transmembrane non-G-protein-signalling receptor which binds the complement activation peptide C5a ligand. The complement cascade is a highly sophisticated network of innate immune proteins that are activated in response to invading pathogens or tissue injury. C5aR2 regulates the release of certain cytokines and is involved in a number of inflammatory conditions. C5aR2 can recruit and form a complex with β-arrestins, which can modulate ERK1/2 signalling in macrophages and neutrophils. C5aR2 has both pro- and anti-inflammatory actions. P32 is a functionally selective C5aR2 ligand which is able to recruit β-arrestin 2 with high efficacy, inhibit C5a-induced ERK1/2 activation and can selectively inhibit LPS-induced IL-6 release from human monocyte-derived macrophages (HMDMs). Functionally selective ligands for C5aR2 such as this are novel tools that can selectively modulate C5a activity and are therefore valuable tools in investigating C5aR2 function.

SARS-CoV-2 NSP7 (21-35)

The coronavirus (CoV) nucleoprotein is the major component of CoV structural proteins. Also known as the nucleocapsid protein, it is an abundant RNA-binding protein critical for viral genome packaging. These factors make nucleoprotein a good target for developing new antiviral drugs. In addition, the identification of epitopes within the nucleoprotein sequence can help design more effective SARS-CoV-2 vaccines.Models have predicted epitopes exhibiting antigenicity, stability and interactions with MHC class-I and class-II molecules. Nucleoprotein (86-100) is an epitope candidate with various HLA restrictions. This epitope can be used to better vaccine design for more durable CD4+ and CD8+ T cell responses for long-lasting immunity.

Ara h 1 is one of the major allergenic proteins from peanut (Arachis hypogaea) which contains approximately 13 potential allergenic proteins.Ara h 1 is a member of the 7/8 S globulin (vicilin) family of seed storage proteins belonging to the cupin superfamily and is the most abundant allergen present in the peanut kernel. Ara h 1 plays an important role in the allergy sensitising procedure and can be recognised by 90% of patients with a peanut allergy.This peptide represents a tryptic peptide of Ara h 1.

Amyloid β-peptide (Aβ) has been identified as the key subunit of the extracellular plaques found in the brains of patients with Alzheimer's disease (AD) and Down's syndrome (DS). Aβ has therefore been extensively studied as a potential target for treatment of AD. Aβ is formed from the cleavage of the large, transmembrane protein- APP (amyloid precursor protein). Cleavage of APP by β- and then γ-secretases results in the formation of Aβ. Aβ can aggregate to produce amyloid-β oligomers, which are thought to be highly neurotoxic. Over time Aβ can further aggregate to produce the characteristic senile plaques present in AD and DS. Aβ can be degraded by enzymes such as neprilysin, insulin degrading enzyme or endothelin converting enzyme. At physiological levels Aβ may be involved in controlling synaptic activity and neuronal survival.

Hyp3-Bradykinin