Peptides

Amino acids 35-55 derived from the Immunogenic Myelin Oligodendrocyte protein (MOG). Produced by oligodendrocytes, MOG is an integral part of the oligodendrocyte surface membrane, located in the central nervous system (CNS) and plays an important role in the maintenance and disintegration of the myelin sheath. Unique within their immunoglobulin superfamily, MOG is composed of a transmembrane hydrophobic domain, an extracellular immunoglobulin variable (IgV) domain, a short cytoplasmic loop and within the membrane bilayer there is a second hydrophobic region and after this, a cytoplasmic end. In addition to 218 amino acids of the mature MOG protein, it contains a 29 amino acids long signal peptide. MOG has not only been found to be expressed in the CNS but also at low levels in the peripheral nervous system. Generally MOG is expressed during myelination and functions to maintain the myelin sheath’s structurally integrity through mediating interactions between the myelin and the immune system. This is possible due to its adhesion characteristics and its external location which makes it accessible to antibodies and T-cells. Furthermore is has been suggested that MOG is involved in regulating oligodendrocyte microtubule stability and it can be used as a differentiation marker for oligodendrocyte maturation.Myelin forms a lipid layer around neurons which insulates them. MOG has immunodmainant epitopes: 1-22; 35-55 and 92-106 and this is located at the dimer interface which is formed by MOG IgV domains forming a dimer. These MOG epitopes are recognized by encepalitogenic T cells as foreign antigens. As a result demyelination occurs and this happens in the disease state of Multiple Sclerosis (MS). As MOG is associated with inflammatory demyelinating diseases within the CNS such as neuromyelitis optica spectrum disorders and acute disseminated encephalomyelitis, this MOG (35-55) product can be used to induce these disease states in animal models. One-Letter Formula: MEVGWYRSPFSRVVHLYRNGK

The myelin sheath which is located in both the Central Nervous System (CNS) and the Peripheral Nervous System is crucial for neural insulation and the salutatory conduction of nerve impulses. When this myelin sheath is destroyed neurodegeneration and conduction failure occur. This can be observed in demyelinating diseases in the CNS such as: acute disseminated encephalomyelitis and multiple sclerosis and within the PNS: Guillain–Barré syndrome and Charcot–Marie–Tooth disease. Myelin Basic Protein (MBP) from which this product is derived is the second most abundant protein in myelin. It has been found to be an intrinsically disordered protein and depending on the environmental conditions it can change its conformation. It also folds into ⍺-helical structures which allow MBP to bind tightly to lipid bilayer surfaces. MBP also interacts with other proteins, namely cytoskeletal proteins and calmodulin and may be involved in signalling pathways. Although more research needs to be carried out, it is thought that MBP significantly contributes to the pathogenesis of multiple sclerosis. As MBP is an autoantigen it can be recognized and cleaved by autoantibodies and is a substrate for the immunoproteasome. Additional research has found that post-translational modifications of MBP such as the removal of arginine are increased in and may be involved in the pathogenesis of multiple sclerosis. Therefore this protein derived from MBP can be used to mimic Neurodegenerative disease phenotypes in research and animal models.

Peptide H-LPASPETHL^DMLR^-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.

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.

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.

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.

An immunoreceptor tyrosine-based activation motif (ITAM) is a phosphorylation site consisting of a conserved sequence of four amino acids that is repeated twice in the cytoplasmic tails of cell-surface non-catalytic tyrosine-phosphorylated receptors. The major role of ITAMs is its involvement in the initiation of signalling pathway and the subsequent activation of immune cells. The motif has the following structure: YxxL/I. where xx are any two amino acids. Two of these signatures are typically separated by between 6 and 8 amino acids in the cytoplasmic tail of the molecule (YxxL/Ix(6-8)YxxL/I). ITAMs are found in the CD3 and θ¶-chains of the T cell receptor (TCR) complex. TCR is a multi-subunit receptor on the surface of T cells. TCR contains two ligand binding chains containing 20 phosphorylation sites, distributed on 10 ITAMs. The TCR θ¶-chain is a homodimer subunit that contains six ITAMs (12 sites). These sites are phosphorylated by the membrane-anchored Src family tyrosine kinase Lck and Fyn and are dephosphorylated by the transmembrane phosphatases CD148 and CD45. When both tyrosines in an ITAM are phosphorylated they generate docking sites for the tandem SH2 domains of the cytosolic tyrosine kinase ZAP-70. Bound ZAP-70 can phosphorylate tyrosines on other substrates that initiate the signal transduction that leads to T cell activation. The multiple ITAMs on the TCR function mainly to amplify subsequent signalling.T cells rely on the TCR to recognize antigens, in the form of peptides bound to major histocompatibility complexes (MHC), on the surfaces of antigen-presenting cells. Binding of TCR to antigen-MCH complexes leads to proliferation, differentiation, and the secretion of effector cytokines, contributing to the elimination of infections.

Apelin-36 (human) is derived from the apelin peptide which acts as a ligand for the apelin receptor (APJ) G protein coupled receptor and is a substrate for angiotensin converting enzyme 2. Preprapelin, encoded for by APLN located on Xq25-26.1, is cleaved to form either apelin 36, apelin 17, apelin 13, or apelin 12. As a member of the adipokine hormone family, which are involved in processes such as vascular homeostasis and angiogenesis, apelin is secreted from adipose tissue.Both apelin and the apelin receptor are widely distributed around the body thus apelin has been found to be associated with cardiovascular diseases, obesity, diabetes and cancer. Studies exploring myocardial infarction showed there to be greater apelin mRNA expression during human heart failure compared to in healthy tissue. Apelin protects against heart failure due to, the pyroglutamyl form of apelin, playing a role in decreasing infarct size of myocardial infarctions. Furthermore in rats with hypertension, the expression of apelin and APJ was decreased.

Hepcidin product containing the disulfide Bonds: Cys4-Cys20, Cys7-Cys10, Cys8-Cys16, and Cys11-Cys19 and available in the trifluoroacetate salt form. Hepcidin-22 is a variant of the peptide hormone hepcidin-25, which plays an important role in the regulation of iron metabolism in the body. Hepcidin is produced by the liver and is secreted into the bloodstream. Hepcidin binds to ferroportin, a protein that facilitates the export of iron from cells into the bloodstream, and to inhibit its activity. The biological significance of hepcidin-22 is still being studied, but it may play a role in the regulation of iron metabolism in certain situations, such as inflammation or certain disease states. Both hepcidin-22 and hepcidin-25 are targets for the development of treatments for iron-related disorders, such as anemia of chronic disease and hemochromatosis.

Peptide H-EQLSSVSSFER^-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.

Fmoc-Thr(tBu)-Wang Resin (100-200 mesh) 1% DVB is a pharmacological research tool that is used to study protein interactions. It is also used as an inhibitor in the synthesis of peptides and has a high purity. This resin can be used for the production of antibodies, which are antibodies that specifically bind to a particular antigen. Fmoc-Thr(tBu)-Wang Resin (100-200 mesh) 1% DVB is an ion channel inhibitor that blocks voltage gated sodium channels, which are involved in pain transmission.

Cyclo(CLLFVY) is a cyclic peptide which binds to the PAS-B domain of HIF-1alpha, thus inhibiting HIF-1 dimerisation and HIF-1 mediated hypoxia signalling.

Peptide derived from tumour necrosis factor alpha (TNF-α), a cytokine produced by macrophages, T lymphocytes and natural killer cells. It exerts its function through targeting the transmembrane receptors TNF receptor 1 and TNF receptor 2, the latter of which it has a higher affinity for. When binding to TNF receptor 1 TNF-alpha is pro-apoptotic and when binding to TNF receptor 2 it is anti-apoptotic. TNF-α has further roles in inflammation, immunity and cancer.Expression of the TNF-α gene, located on chromosome 6 in humans is regulated by factors such as nuclear factor kappa b (NFKB).Dysregulation of TNF-α and its receptors can contribute to diseases such as rheumatoid arthritis, Crohn disease and diabetes. Anti-TNF-α can be used as a therapeutic agent to target TNF-α during inflammatory diseases.

A synthetic peptide for use as a blocking control in assays to test for specificity of BTN2A1 antibody, catalog no. 70R-7238

Peptide 5Fam-FLPSDCFPSV-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.