Péptidos

<p>Infliximab is a biologic medicine used in the treatment of numerous autoimmune diseases including Crohn disease, rheumatoid arthritis, and ankylosing spondylitis. Infliximab binds with high affinity to tumour necrosis factor-α (TNF-α) blocking most of the cytokine effects, which includes mediating the inflammatory responses. Infliximab is a chimeric human-mouse IgG monoclonal antibody- the constant regions of the heavy and light chains are human-derived. The heavy chain peptide (46-60) has been identified as an antigen for antigen-specific T cell analysis. Numerous methods of immunological analysis can be applied to this peptide to hopefully provide further insight to these autoimmune conditions.</p>

<p>Glucagon (1-29)-[Cys(Cy5)] is derived from glucagon, which is a peptide hormone secreted by alpha cells located in the islet of Langerhans region of the pancreas. Glucagon is an essential catabolic hormone that is responsible for the regulation of blood glucose levels. Once released into the bloodstream, glucagon stimulates the production of hepatic glucose, which means it is considered to be a glucose-mobilizing agent. Excessive levels of glucagon can result in the development of hyperglycaemia, since the action of glucagon results in abnormally high blood glucose levels.This peptide contains Cyanine 5 (Cy5), which is a widely used red fluorescent dye.</p>

<p>Histone H3 (1-20)-[S]-Biotin 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.Another modification process histones can undergo is biotinylation where the covalent attachment of a biotin molecule is catalysed by the enzyme Biotinidase. This cleaves biocytin to generate a biotinyl-thiester intermediate. The biotinyl can then be transferred onto the histone lysine ɛ-amino group which in this case it is covalently attached to Histone 3. Overall the biotinylation sites identified in histone 3 are: K4, K9 and K18. The presence of biotinylated histones have been detected in human cells such as lymphocytes and lymphomas.</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>Identification of cell penetrating conjugates has aided numerous areas of scientific development. The Drosophila transcription factor Antennapedia contains a homeodomain that can be internalised by cells to the cytoplasm and to the nucleus in a receptor-independent mechanism. The key residues for internalisation have been sequenced (RQIKIWFQNRRMKWKK), named penetratin, and used in several studies to aid entry of fusion proteins into cells.The full 60 amino acid homeodomain was fused to a T cell epitope of the influenza nucleoprotein and successfully internalised into T cells for presentation. The CPP, penetratin, was fused to a ligand for Grb-2 resulting in inhibition of downstream Grb-2 signalling events.- Penetratin has also been used in vivo to prime cytotoxic T lymphocytes by conjugating short antigenic peptides to the CPP. Penetratin is provided here as a C-terminal acid but is also available in amide form.</p>

<p>This 32 amino acid peptide contains a 17 amino acid ring structure that is common to all natriuretic peptides. It is also called the brain natriuretic peptide (BNP) because it was first identified in porcine brain- however, the main source of this peptide is not the brain but the cardiac ventricle. This cardiac neurohormone is secreted from the ventricles in response to volume expansion and pressure overload. It has natriuretic and vasodilatory effects and suppresses the renin-angiotensin-aldosterone system.</p>

<p>(RXR)4XB is a cationic membrane-penetrating peptide and is effective in delivering phosphorodiamidate morpholino oligonucleotides (PMOs) into eukaryotic cells such as Escherichia coli. It contains 5-carboxyfluorescein (5-FAM), a widely used green fluorescent tag.</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.The MOG (34-56) fragment is in the most potent auto-antigenic region of MOG, and is highly effective at inducing experimental autoimmune/allergic encephalomyelitis (EAE), an animal model that resembles MS. This peptide has an uncharged C-terminal amide.</p>

<p>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 (371-382) is a class I (Kb)-restricted peptide epitope of OVA. The ovalbumin fragment is presented by the class I MHC molecule, H-2Kb.</p>

<p>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 gradual 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.Treatments of dystrophin disorders are in clinical trial including antisense oligonucleotide exon skipping and gene therapy. However, the efficacies of these treatments are not easily quantified. Currently levels of muscular dystrophin are quantified by western blot which can be unreliable. The peptide provided here, aligning residues dystrophin (2690-2700), has been tested via western blot, mass spectrometry, immunostaining and RT-PCR to try and provide the most robust method of validation of dystrophin levels possible. Further study with this dystrophin fragment could prove to be a vital step in the understanding and treatment of dystrophin disorders. Within our catalogue we also have other peptides tested for dystrophin quantification available plus the full-length dystrophin protein.</p>

<p>Identification of cell penetrating conjugates has aided numerous areas of scientific development. The Drosophila transcription factor Antennapedia contains a homeodomain that can be internalised by cells to the cytoplasm and to the nucleus in a receptor-independent mechanism. The key residues for internalisation have been sequenced (RQIKIWFQNRRMKWKK) and used in several studies to aid entry of recombinant proteins into cells. The peptide sequence described, known as penetratin, was fused to a ligand for Grb-2 resulting in inhibition of downstream Grb-2 signalling events.- Penetratin has also been used in vivo to prime cytotoxic T lymphocytes by conjugating short antigenic peptides to the cell penetrating peptide.On this sequence the N terminal active cysteine has been protected by a 3-Nitro-2-pyridinesulfenyl group. This is a useful modification as it allows this peptide to be used as a carrier peptide in conjugation reactions- this is a particularly useful modification when the peptide-like molecule contains a free thiol group.</p>

<p>AD01 is a derivative of the FK506 binding protein-like (FKBPL), and exerts potent anti-angiogenic activity in vitro and in vivo to control tumour growth. Recent studies have shown that AD-01 inhibits Rac-1 activity, and up-regulates RhoA and the actin binding proteins, profilin and vinculin. In this way, the anti-angiogenic proteins, FKBPL, and AD-01, offer a promising and alternative approach for targeting both CD44 positive tumours and vasculature networks. Recent clinical studies have shown that AD01 and other FKBPL-based peptides may offer an alternative for targeting treatment-resistant breast cancer stem cells.</p>

<p>N-terminal tryptic peptide of parathyroid hormone (PTH), used for quantification and optimisation in LC-MS/MS assays.PTH is an 84-amino-acid polypeptide hormone (PTH 1-84) which is secreted by the parathyroid glands along with its fragments (such as PTH 1-34 and PTH 7-84). PTH increases calcium and decrease phosphate levels in the blood and the abundance of PTH-derived peptides is regulated by blood calcium levels. PTH inhibits the bone growth-promoting activity of osteoblasts and induces osteoclasts to resorb bone and release calcium and phosphate ions into the blood. PTH binds to and activates the receptor parathyroid hormone receptor 1 (PTHR1). PTHR1 is a G-protein-coupled receptor (GPCR) which regulates mineral ion homeostasis, bone turnover and skeletal development</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>Bovine myeloid antimicrobial peptide-27 (BMAP-27) belongs to the cathelicidin family of peptides which displays rapid bactericidal activity against Staphylococcus aureus, Streptococcus uberis, and Escherichia coli. Cathelicidins belong to the large group of cationic peptides with amphipathic properties and have an important role in the mammalian innate immune system. BMAP-27 is cytotoxic to human erythrocytes and neutrophils, although at higher than microbicidal concentrations. It has a potential for the treatment of bacterial infections in individuals with cystic fibrosis-associated lung infections.</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>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>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>Orexin B is one of two closely related peptides- the orexins (also known as hypocretins). These small neuropeptides are secreted from orexin-containing neurons, located mainly in the lateral hypothalamus (LH). Orexins function via the binding and activation of two G-protein-coupled receptors (GPCRs)- orexin receptor type 1 (OX1) and 2 (OX2).[Ala(11), D-Leu(15)]orexin-B is a highly potent and selectiveOX2 receptor agonist which can discriminate between the OX1 and OX2 receptors, with a 400-fold selectivity for the OX2 over OX1. [Ala(11), D-Leu(15)]orexin-B is therefore a beneficial tool for addressing the functional roles of OX2.The L-leucine residue at position 11 of orexin B is important for selectivity to OX2 over OX1. L-Alanine substitution at position 11 and D-leucine substitution at positions 15 maintain the potency of orexin-B to OX2, while significantly reducing the potency for OX1.Orexins play several vital roles in a range of physiological activities, including: circadian rhythm- feeding behaviour- energy balance- glucose metabolism- neuroendocrine functions- stress-adaptive responses and reward and addiction. Orexins have also been linked to the pathological processes of neurological diseases such as: narcolepsy- depression- ischemic stroke- drug addiction and Alzheimer's disease.</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>

Peptide H-YTFELSR^-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>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>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>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>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>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>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)alanine residues as acyl acceptors, 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 C-terminal biotin tag for detection and purification.</p>

<p>Cell-penetrating peptides (CPPs) have the ability to cross cell membrane bilayers without causing lethal membrane damage. CPPs themselves can exert biological activity and can be formed endogenously, or alternatively they can enhance transport of different cargoes across cell membranes. Vascular endothelial-cadherin-derived peptide (pVec) is an amphipathic CPP, these are characterised by both hydrophobic and hydrophilic regions. The charged region interacts with the cell membrane, while the hydrophobic region causes membrane perturbation, enabling translocation. pVec is derived from vascular endothelial cadherin, which is able to cross the blood brain barrier. Peptide is labelled with an N-terminal 5-carboxyfluorescein (5-FAM), a widely used green fluorescent tag.</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>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>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>Galanin is predominantly an inhibitory neuropeptide expressed in humans and other mammals' brains, spinal cords, and gut. Galanin signalling occurs through three G protein-coupled receptors. The functional role of galanin remains largely unknown- however, galanin is predominantly involved in the modulation and inhibition of neuron action potentials. Galanin has been implicated in many biologically diverse functions, including nociception, waking and sleep regulation, cognition, feeding, mood regulation and blood pressure regulation. Galanin appears to have neuroprotective activity as its biosynthesis is increased 2-10 fold upon axotomy and during seizure activity in peripheral tissues and the brain.The clinical relevance of galanin is related to several chronic neural disorders, including Alzheimer's disease, epilepsy, depression and cancer those who suffer from type 2 diabetes mellitus, depression and Alzheimer's disease often express high levels of galanin. Conversely, intervention with galanin agonists (for example, M617, M1145 and M1153) manifests anti-insulin resistance and anti-Alzheimer's disease characteristics and ameliorates or reinforces depression-like behaviour. Specifically, activation of GAL2 can alleviate such disease features in human and rodent models. This galanin (2-30) peptide has been used to characterise Galanin's binding sites and affinity for GALR receptors via competition binding analysis. Galanin (2-30) is a full agonist of the GALR2 receptor compared to its affinity for GALR1.Galanin (2-30) is provided with an N-terminal 5-FAM, a widely used green fluorescent reagent ideal for peptide labelling and detection and a C-terminal cysteine for site-specific conjugation. The excitation/emission for this reagent is 490 nm/520 nm.</p>

<p>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.</p>

<p>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.</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>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.</p>

<p>Fluorescently labelled substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro).- The substrate sequence is derived from residues P4-P5' of the SARS-CoV Mpro-N-terminal autoprocessing site which has the sequence AVLQSGFRK. SARS-CoV Mpro is a key antiviral target.This peptide contains a highly fluorescent N-terminal 7-methoxycoumarin fluorophore (Mca) and a 2,4-dinitrophenyl (Dnp) quencher. Mca is efficiently quenched by resonance energy transfer to the 2,4-dinitrophenyl group when the peptide is intact, however upon cleavage of the peptide by Mpro, the Mca group and the Dnp quencher are separated and fluorescence can be detected. This therefore represents a useful tool for investigating Mpro activity.</p>

<p>Osteogenic Growth Peptide (OGP) is derived from the C-terminal sequence ALKRQGRTLYGFGG of Histone H4. This 14-aa peptide is produced from alternative translation of Histone H4 mRNA.</p>

<p>Galanin (1-30) (human) is an endogenous neuropeptide with endocrine, metabolic and behavioural effects. Galanin has a role in intestinal smooth muscle contraction, insulin and somatostatin release, and synaptic neurotransmission.Galanin is widely distributed in the central nervous, peripheral, and endocrine systems. Galanin's overarching function is as an inhibitory, hyper-polarizing neuromodulator for classical neurotransmitters like acetylcholine and serotonin. Galanin interacts with 3 receptor subtypes, GalR1-3 G protein-coupled receptors inserted into the plasma membrane. GalR1 is believed to activate a Gβγ pathway to regulate MAPK activation. GalR2 can also activate the MAPK pathway, but unlike GalR1, there is detectable inositol phosphate production. GalR3 is associated with the Galphai/o pathway. Activation of the receptor leads to a cellular influx of K+. Each receptor has been associated with neurological diseases such as GalR3 and epilepsy.Galanin protects against various physiological insults in vitro, including excitotoxicity and β-amyloid toxicity. Changes in galanin have been widely studied concerning Alzheimer's disease, and galaninergic neurons are spared in late-stage Alzheimer's relative to non-galaninergic neurones.Galanin (1-30) has been used as an agonist for the GalR2 receptor in vitro for calcium mobilisation assays to understand the role Galanin/GalR2 play in multiple sclerosis.Galanin (1-30) is provided with an N-terminal 5-TAMRA, a widely used red fluorescent reagent ideal for peptide labelling and detection. The excitation/emission for this reagent is 555 nm/580 nm.</p>

<p>The SARS-CoV-2 spike protein is present on the outside of the virus particles and can bind to angiotensin-converting enzyme II (ACE2) present on the host cells. The C-terminal receptor binding domain (RBD) of the spike protein binds to the N-terminal peptidase M2 domain of ACE2. This receptor binding results in the internalisation of the virus-receptor complex and is, therefore the mechanism of entry of SARS-CoV-2 into host cells.The spike protein residues LIDLQELGKY (1197-1206) 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>The RGD peptide is a ligand for cell-surface integrin receptors, which are used by most cells to attach to and sense the extracellular environment and to establish a cytoskeleton. RGD peptide can be attached to biologically important molecules, such as nanoparticles, to enable active targeting of drugs or gene delivery. Model substrates presenting immobilised RGD peptide can be used to promote the adhesion and spreading of cells which have been engineered to expresses integrin receptors such as the platelet cell-surface integrin receptor, alphaIIbβ3. Cells growing in these conditions appear to have well developed cytoskeletons suggesting that binding to the integrin receptor mediates biologically relevant adhesion and RGD substrates are able to support cell survival. Peptide is labelled with an N-terminal 5-carboxyfluorescein (5-FAM), a widely used green fluorescent tag.</p>

<p>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.</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>SARS-CoV-2 NSP13 (336-350)</p>

<p>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.</p>

<p>H-STMSIT-OH peptide, corresponding to RNase A 77-82 (Chain A of bovine pancreatic ribonuclease) has been published to have amyloidogenic properties, and under certain conditions H-STMSIT-OH hexapeptide forms amyloid fibrils. Please also see CRB1001321, which you can use as a negative control in amyloid formation experiments.</p>

<p>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.</p>

Peptide H-KQL^ATKAAR-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>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.</p>

<p>Myocarditis is an inflammatory heart disease often associated with a previous viral infection. Evidence has suggested that myocarditis may be due to autoimmune responses directed against cardiac tissue. The inflammatory immune response caused after infection may break tolerance by mechanisms of molecular mimicry, bystander activation, and loss of immune regulation. Experimental autoimmune myocarditis (EAM) is a model of inflammatory heart disease generated by immunizing susceptible rats or mice with cardiac myosin or its myocarditic epitopes. In the EAM model, cellular infiltrates consist primarily of T cells and macrophages, and T lymphocytes responsive to cardiac myosin can transfer disease. Cardiac myosin is a large peptide, which is composed of two H chains and two pairs of L chains. Proteolysis of myosin yields three subfragments including a globular head or subfragment 1 (S1) region, an alpha helical coiled coil rod comprised of subfragment 2 (S2), and light meromyosin (LMM). In the Lewis rat, the S2 subfragment has been shown to produce the most severe myocarditis.</p>