Peptides

<p>Histone H3 (1-20) K4Me3 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.Lysine 4 of H3 (1-20) has been tri-methylated.</p>

<p>The P11-family of peptides comprises over 20 different peptides which self-assemble into β-sheet structures to form self-supporting isotropic hydrogels under physiological conditions (pH 7.4, 140 mM NaCl). Self-assembling peptides of the P11-family undergo one-dimensional self-assembly, forming single molecule thick, micrometer-long β-sheet nanotapes. Further assembly results in the nanotapes stacking in pairs to form ribbons which further assemble to form fibrils, then pairs of fibrils can entwine to form fibres. Such self-assembling peptides are important biomaterials and may be useful for the development of novel biomaterials for tissue engineering scaffolds and dental enamel remineralisation.</p>

<p>The SOD1 homodimer forms a β-barrel and contains an intramolecular disulphide bond and a binuclear Cu/Zn site in each subunit. This Cu/Zn site holds a copper and zinc ion and is responsible for catalysing the disproportionation of ROS, namely superoxide to hydrogen peroxide and dioxygen. In binding to copper and zinc ions, SOD1 is one of three superoxide dismutases responsible for destroying free superoxide radicals.The clinical relevance of SOD1 is related to its function in regulating ROS in the mitochondria of cells. Most notably, SOD1 is a crucial enzyme involved in ROS release during oxidative stress by ischemia-reperfusion injury, specifically in the myocardium as part of ischemic heart disease. During ischemia reperfusion, ROS release substantially contribute to the cell damage and death via a direct effect on the cell as well as via apoptotic signals. SOD1 is known to have a capacity to limit the detrimental effects of ROS. As such, SOD1 is important for its cardioprotective effects.</p>

<p>Spexin is a neuropeptide encoded by SPX genes, and homologs have been found amongst many vertebrates. The SPX genes encode a preprohormone that leads to the mature hormone spexin, which is highly conserved amongst higher vertebrates. Another form, SPX2, has been identified and named spexin 2. Both sequences of spexin and spexin 2 are highly conserved, suggesting they each play vital roles.Like spexin, spexin 2 is widely expressed in various tissues. This is an amidated spexin-2 (53-70) peptide showing similar biological function to its non- amidated version. Spexin-2, when administered to rats, decreases heart rate and increases urine flow rate. Intraventricular NPQ(53-70) delivery also causes antinociceptive activity in mice's warm water tail withdrawal assay.</p>

<p>Biotin gliadin-derived peptides derived from Gliadin peptides, the component of wheat involved in the gastrointestinal symptoms of wheat allergy and Celiac Disease (CD). During wheat allergies histamines and leukotrienes are secreted due to gliadin peptide sequences cross-linking two IgE molecules on mast cells and basophils.The glutamine and proline rich peptides of which Gliadin is composed of are resistant to proteolysis during digestion, leaving them active in the gastrointestinal tract. Subsequently these are deamidated by tissue transglutaminase and can bind to HLA-DQ2 or DQ8. As a result in patients with the autoimmune disease CD, there is a Th-mediated inflammatory immune response against these gliadin peptides.Gliadin can exert additional effects on the intestinal microbiota and ileal barrier function. It has been found that gut microbiota members such as Bifidobacterium and lactobacillus have the ability to digest and inactivate gliadin peptides hence reducing their inflammatory effects in the gastrointestinal system.Here Biotin (B7) has been added. Biotin is a cofactor for several mammalian biotin-dependent carboxylases which are involved in processes such as gluconeogenesis, amino acid metabolism and fatty acid synthesis.</p>

<p>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.</p>

<p>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.</p>

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

<p>Human adrenocorticotropic hormone (ACTH), also known as corticotropin, 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. ACTH (15-24) has been shown to be a competitive ACTH receptor antagonist and can be used as a method to combat the overproduction of cortisol. Treatment with ACTH (15-24) inhibits activation of a specific melanocortin 2 receptor (MC2R) by inhibiting adrenocorticotropin hormone (ACTH)-induced production of cortisol. ACTH (15-24) is provided here with a C-terminal cysteine residue for conjugation reactions.</p>

<p>Apidaecin IB was isolated from the honeybee Apis mellifera. As a cationic proline-rich antimicrobial peptide (PrAMP), Apidaecin IB shows sequence homology with drosocin but is devoid of any pore-forming activity. Apidaecin IB is most active against gram-negative bacteria, it can navigate the outer membrane to the periplasm and then to the cytoplasm. Apidaecin IB is a non-lytic AMP, the main target of its antimicrobial activity appears to be inhibition of the chaperone heat shock protein DnaK. Toxicity appears to be exclusively to bacteria and thus has been trialled as a treatment for systemic bacterial infections. Numerous analogues and derivatives are being investigated to establish Apidaecin IB mode of action and also to improve its functionality.</p>

<p>Gag peptide, derived from the simian immunodeficiency virus (SIV), is a homologue of the human immunodeficiency virus (HIV) gag protein which interacts with viral components in order to induce the infectious form of the virus. SIV can be used to model HIV.</p>

<p>Histone H3 (1-20) K4Me3, K9Ac-GG-[Lys(5-FAM)] is derived from Histone 3 (H3) which is one of the four core histones fundamental for compacting eukaryotic DNA into the nucleosome.-Lysine 4 of Histone H3 (1-20) K4Me3, K9Ac-GG-[Lys(5-FAM)] has been tri-methylated, lysine 9 has been acetylated and the C-terminal has been labelled with 5-Carboxyfluorescein (5-FAM), a widely used green, fluorescent tag. Additionally, this peptide contains an uncharged C-terminal amide.LD: Histone H3 (1-20) K4Me3, K9Ac-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. The lysine at position 9 has been acetylated, which neutralizes the positive charge on the amino acid, loosening the chromatin structure. This alteration to the accessibility of chromatin promotes the initiation of transcription.Additionally, Histone H3 (1-20) K4Me3, K9Ac-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.</p>

<p>H1 is the linker histone and is important for chromatin condensation, it binds to the nucleosomal core particles and protects the free linker DNA (ˆ¼20 bp) between each nucleosome. H1 can fine-tune transcription in a locus-specific manner. H1 is involved in several processes, its interaction partners include: pre-mRNA splicing factors- histone chaperones- components of the transcription machinery and DNA-damage response factors. There a 12 subtypes of the H1 linker histone, and they are thought to have specific functions, making H1 the most divergent histone protein family. Like other histones, H1's are extensively post-translationally modified with modifications including: methylation, acetylation, ubiquitination, formylation, poly-ADP ribosylation and phosphorylation.Changes in H1 composition and expression levels are seen in several cancers and other diseases.</p>

<p>The Histone H2A residues 1 to 20 are derived from histone 2A (H2A) 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.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.Biotin has been added to the lysine on GGK.</p>

<p>Orexin-A (also known as hypocretin-1) is a hypothalamic neuropeptide that regulates feeding behaviour, reward processes, cognition, the sleep-wake cycle and stress. Orexin-A is involved in stress induced mental illness such as major depressive disorder and anxiety disorders and may therefore be a potential target for treatment of these conditions.Orexins are excitatory neuropeptides generated from the prepro-orexin precursor that is exclusively localised in cells of the lateral and posterior hypothalamic region. Orexins are also widely expressed in human and mammalian retinas, such as bipolar cells, amacrine cells and ganglion cells.Orexin-A activates the orphan G-protein-coupled orexin receptor, type 1 (OX1R) and 2 (OX2R). There are approximately 10,000-20,000 orexinergic neurons in the human brain.</p>

<p>LP2</p>

<p>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 (556-570) 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.</p>

<p>Pantinin-3, like other pantinin peptides, has high activity against Gram-positive bacteria yet weak activity against Gram-negative bacteria. With the exception of S. aureus, pantinin-3 displays the highest activity against all Gram-negative bacteria for which it has been tested. Pantinin-3 also displays activity against Candida tropicalis and has relatively mild haemolytic activity against human red blood cells.</p>

<p>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. Hepatitis B virus (HBV) polymerase is a multifunctional enzyme that can use both RNA and DNA as a template for amplification and also has an RNase H function. First the polymerase acts on the HBV pre-genomic RNA (pgRNA) to reverse transcribe it to form the (-) DNA strand. Simultaneously the RNA template is degraded by the polymerases RNase H activity, except for a stretch of RNA at 5' end of the pgRNA which is used to prime the synthesis of the (+) DNA strand. This process results in a new partially double-stranded relaxed circular DNA molecule (rcDNA) within a new capsid.</p>

<p>Residues 1-16 of the gastrointestinal hormone motilin, secreted from endocrine cells in the small intestines, mainly from the jejunum and duodenum, in response to the fasting, drinking water or the mechanical stimulus of eating.</p>

<p>The coronavirus (CoV) nucleoprotein is the major component of CoV structural proteins. The nucleoprotein has a critical role in virus assembly and RNA transcription. The nucleoprotein is essential in the formation of helical ribonucleoproteins and in regulating viral RNA synthesis. The nucleoprotein can also regulate infected host cellular mechanisms. It is highly expressed during infection and may induce protective immune responses against SARS-CoV and SARS-CoV-2.The nucleoprotein residues TQAFGRRGPEQTQGN (271-285) from SARS-CoV-2 have been identified as a T-cell epitope with a predicted HLA restriction. Immune targeting of confirmed epitopes may potentially offer protection against SARS-CoV-2 and help the development of vaccines for long-lasting immunity.</p>

<p>Boc-VPR-AMC is a fluorogenic peptide substrate composed of the short peptide chain, Valine-Proline-Arginine (VPR) and the fluorophore, 7-amino-4-methlycoumarin (AMC). Fluorogenic peptide substrates such as Boc-VPR-AMC have high sensitivity and specificity and therefore can be used to detect molecules of interest. For example within the field of scientific forensics, Boc-VPR-AMC can be used to investigate deposits of saliva in situ. When Fluorogenic peptide substrates are incubated with specific enzymes, fluorescence is emitted due to the release of the fluorophore from the peptide-fluorophore bond. When Boc-APR-AMC interacts with its target enzyme, the 7-amino-4-methylcoumarin fluorophore is released causing a fluorescent emission at 440nm.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Model substrate peptide for heat shock protein 70 (HSP70)/ Chaperone protein DnaK. Binds to the substrate binding domain of DnaK and is used in co-crystallisation assays. DnaK is the most well studied heat shock proteins and is central in protein folding and in shuttling misfolded peptides to other chaperones and proteases for resolution. In the presence of ADP, this substrate peptide interacts with DnaK with high affinity, however when ATP is bound to DnaK, substrate binding is far weaker.</p>

<p>Inhibitor of HIV-1-mediated cell-cell fusion in a dose-dependent manner, and exhibits high potency against infections by a wide range of primary and laboratory-adapted HIV-1 isolates from multiple genotypes. Highly effective against T20 resistant strains.</p>

<p>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.</p>

<p>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.</p>

<p>Kallikrein-2 inhibitor</p>

<p>Portion of HCMV pp65</p>

<p>Peptide H-FSTPPGELDGGISGR^-OH 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.</p>

<p>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</p>

<p>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.</p>

<p>Portion of EBV</p>

<p>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.</p>

<p>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.</p>

<p>Pyroglutamyl β-Amyloid (4-14) Biotin is derived from Amyloid-β, which 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.This peptide contains a C-terminal Biotin tag that is covalently bonded via ethylenediamine and can be used for detection and purification. Additionally, there is a Pyroglutamyl molecule located at the N-terminal position.</p>

<p>[Sulfo-Cyanine3]-LifeAct (Abp140 1-17) contains the fluorophore sulfo-cyanine3 and the 17 amino acid peptide lifeact derived from amino acids 1-17 of the Saccharomyces cerevisiae actin binding protein, Abp140. These first 17 amino acids of Abp140 are crucial in allowing lifeact to localise to actin filaments (F-actin) and therefore it can be used as a cytoskeletal marker. One application of lifeact is in the study of plant development and pathogen defence as filamentous actin within the plant's actin cytoskeleton is important in key processes such as cell division, membrane trafficking and stomatal movements. The addition of Atto655 which has single molecule (SM) imaging properties allows the location of lifeAct (Abp140 1-17) binding to be detected.</p>

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

<p>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 autoantibodies and cell-mediated immune responses in inflammatory demyelinating diseases such as multiple sclerosis (MS) and is therefore widely studied in this field.Fragment 92-106 of MOG is able to induce experimental autoimmune/allergic encephalomyelitis (EAE), an animal model that resembles MS.</p>

<p>Represents the extracellular region of amyloid β peptide (Aβ). This region may be responsible for the conformational changes seen in Aβ and is cytotoxic in vitro.Aβ has been identified as the key subunit of the extracellular plaques found in the brains of patients with Alzheimer disease (AD) and Down 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 &amp;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.</p>

<p>Eα antigen peptide, known to bind with high affinity to the major histocompatibility complex (MHC) class II molecule IAb. MHC class II molecules are normally found on antigen presenting cells such as dendritic cells, mononuclear phagocytes, endothelial cells, thymic epithelial cells and B cells and they present antigens derived from extracellular proteins. Eα peptide bound to IAb is specifically recognized by Y-Eα antibody.This peptide contains a C-terminal biotin tag for simple detection and purification.  The linker is ethylenediamine.</p>

<p>The progress of cardiovascular disease (CVD) comes from the damage and necrosis of cardiomyocytes. Although treatment has improved, once these cells are damaged, they cannot be recovered. Therefore, further research into cardiomyocytes is vital. Cardiomyocytes need to be in an exceedingly pure culture for research work. However, this requires identification of these cells from the ESCs present. With the use of a phage biopanning library, this sequence has been shown to have a high affinity to a receptor on the membrane surface of mouse ESC-derived cardiomyocytes. The functionality of this sequence allows it to be used a conjugate for drug or gene delivery to target cardiomyocytes or to purify cardiomyocytes in a research setting.</p>

<p>Peptide derived from vitronectin, the mammalian glycoprotein which plays a key role in tissue repair and remodelling. Its properties as an adhesive protein allow mammalian cells in serum to interact with culture vessels.</p>

<p>HIV-1 replication is rapid and error prone which is beneficial to the virus as it allows mutations to arise that aid evasion of the host immune system and resistance to drug treatment. RT is the key target for most anti-HIV drugs and therefore conserved sequences are useful to aid further research into new less toxic antiviral treatments.  HIV-1 reverse transcriptase (RT) converts the RNA genome into DNA during retroviral replication. HIV-1 RT is a heterodimer composed of 2 subunits, p66 and p51. HIV-1 RT heterodimer has 2 enzymatic functions, DNA polymerase and Rnase H resulting in nucleic acid translation to a linear DNA duplex. Complete inhibition of viral replication is the only known method of preventing HIV-1 drug resistance and disease progression.HIV RT epitopes have become a useful research tool as an in vitro antigenic challenge to study cytotoxic T lymphocyte (CTL) responses to retroviruses. The HIV-1 RT A2-YI9 sequence has been shown to be an effective epitope for CTL recognition leading to lysis of HIV-infected T cells. The A2-YI9 is also considered a potential for vaccine development due to it being a well conserved sequence. Synthesised HIV-1 RT A2-YI9 is provided here with N-terminal acetylation to mimic the charge of the native peptide more closely. The epitope is also available without acetylation from our catalogue.</p>

<p>Cyclic AC253 is an antagonist of the amylin receptor with neuroprotective effects against Aβ toxicity. Cyclic AC253 eliminates Aβ-induced impairment of hippocampal long-term potentiation and is able to penetrate the blood-brain barrier.</p>

<p>This C-terminal Sortagging peptide acts as a (oligo)glycine nucleophile in the final steps of a sortagging protein labelling reaction. This reaction results in the [Cys(AF488)] fluorescent moiety being attached to the C-terminus of the target protein or peptide.A substrate peptide containing the LPXTG motif 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 of the substrate peptide. Cleavage results in the formation of a thioacyl intermediate between the substrate peptide and SrtA. This intermediate is then resolved by the N-terminus of this (oligo)glycine nucleophile peptide, resulting in the creation of a new peptide bond that links the substrate peptide to this peptide and its fluorescent dye.  This method of protein labelling is known as sortagging.This peptide contains the AF488 fluorescent dye AF488 is a bright green dye with excitation at 488 nm, it is water soluble and stable from pH 4 to pH 10.</p>

<p>EBV BRLF1 (148-156) (HLA-A3) is an immunodominant CEF control peptide that is derived from the Epstein-Barr virus (EBV). EBV targets B cells, which can cause lytic infection and the consequent death of these cells. Natural killer (NK) cells, invariant (iNKT) cells, CD4T cells and CD8 T cells are essential to control the action of EBV-infected cells. EBV BRLF1 (148-156) (HLA-A3) is defined as a CEF control peptide due to its antigenic properties. Clinically, this peptide is a suitable epitope for CD8+ T cells and can be used to stimulate the release of IFNg. HLA-A3 refers to the cell HLA type that this peptide acts on.The BRLF1 protein is a transcriptional activator that interacts with the amino and carboxy termini of the CREB-binding protein (CBP). CBP activates the lytic EBV gene SM, meaning the interaction between CBP and BRLF1 is responsible for EBV particles switching from latent to lytic viral replication.</p>

<p>Portion of Influenza NP</p>