Peptidi

Peptide α-Neo-Endorphin, porcine 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.

Peptide LCBiot-VTSAPDTRPAPGSTAPPAHG-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.

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.

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.

CREB is a transcription factor that regulates diverse cellular responses including: proliferation- survival and differentiation- adaptive immune responses- glucose homeostasis- spermatogenesis- circadian rhythms and synaptic plasticity associated with memory. CREB is induced by a variety of growth factors and inflammatory signals and subsequently mediates the transcription of genes containing a cAMP-responsive element, including IL-2, IL-6, IL-10, and TNF-alpha. In the immune system, CREB induces an anti-apoptotic survival signal in monocytes and macrophages, has a role in promoting the proliferation, survival and regulation of T and B lymphocytes and is required for the generation and maintenance of regulatory T cells. CREB also often promotes anti-inflammatory immune responses, such as through the inhibition of NF-KB activity, the induction of IL-10, and the generation of Tregs. These anti-inflammatory responses could be protective by inhibiting unwanted inflammation, tissue damage, and autoimmune responses, or they could be pathogenic in the context of infection and tumour immunosurveillance. Peptide is labelled with an N-terminal 5-carboxyfluorescein (5-FAM), a widely used green fluorescent tag.

Peptide H-AVQVHQDTLR^-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.

Peptide H-AVTEQGAELSNEER^-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.

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.

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.

Reactivity to human leukocyte antigens (HLAs) is a risen concern in clinical treatments such as organ transplant rejection. Understanding the epitopes causing reactivity and the signalling pathways could lead to better clinical therapies. The peptides presented by the non-classical HLA-G are important for a largely tolerogenic role and are considered part of an immune checkpoint. This, therefore, makes understanding ligand characteristics and HLA-G a target for cancer therapies. The HS1 fragment (160-168) has been identified as an epitope that human leukocyte antigen HLA-G naturally presents, determined by liquid chromatographic tandem mass spectrometry (LC-Ms/MS). This epitope has been used extensively in the literature to help understand the natural ligand presentation of HLA-G.For example, leukocyte immunoglobulin (Ig)-like receptors (LILRs) are key regulators of the immune response and therefore targets for therapeutics. Inhibitory LILRB1 and LILRB2 with HLA-G are pivotal for immunotolerance during pregnancy and autoimmune diseases plus cancer cell immune evasion. HS1 fragment (160-168) was used in binding affinity assays to clarify the conformational plasticity of the interaction between the receptor, the HLA antigen, and the various peptides HLA-G can accommodate.

Fluorescence resonance energy transfer (FRET) peptide substrate derived from SARS-CoV-2 spike (S) S1/S2 site. This FRET peptide exhibits internal fluorescence quenching when intact, however hydrolysis of the peptide between the donor/acceptor pair generates fluorescence, enabling the quantitative measure of enzymatic activity. The S1/S2 site of SARS-CoV-2 S is efficiently cleaved by a wide range of proteases including furin.SARS-CoV-2 Spike (S) protein is one of the four essential structural proteins from the coronavirus SARS-CoV-2. S protein is a large, class I viral transmembrane protein essential for viral entry into the cell via binding to the host angiotensin-converting enzyme 2 (ACE2) receptor. S assembles as a trimer on the surface of the virion, giving it its distinctive 'corona' or crown-like appearance. The ectodomains of S proteins are divided into two subunits, S1 and S2. S1 helps in host receptor binding and is further divided into two subdomains: N-terminal domain (NTD) and C-terminal domain (CTD), both of which act as receptor-binding domains. The S1 CTD contains the receptor-binding motif (RBM). The S2 subunit accounts for fusion. Peptide contains an N-terminal 5-carboxyfluorescein (5-FAM), a widely used green fluorescent tag and a 2, 4-dinitrophenyl (Dnp) quencher.

C-type natriuretic peptide (CNP) is expressed from numerous tissue types but primarily within the central nervous system and the bone. CNP binds the natriuretic peptide receptor B (NPR-B) and acts as an autocrine/paracrine factor. CNP signalling acts as a positive regulator of endochondral bone growth. Both CNP and NPR-B are being explored as therapeutic targets for growth disorders including achondroplasia. CNP (1-22) is the major form of CNP found in the plasma. Exogenous CNP (1-22) can be cleared quite effectively, administration of a constant 'high' dose was able to overcome this obstacle to induce endochondral ossification and accelerated bone growth. However, CNP (1-22) may have the potential to induce systemic vascular resistance and blood pressure issues which would need to be addressed before future clinical applications. Researchers are trying to better establish the function and role of CNP (1-22) one strategy has been the addition of conjugates, such as the C-terminal of ghrelin, to try and improve the clinical efficacy.

Peptide LCBiot-SPDVDLGDISGINAS-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.

Peptide H-DPGVLDR^-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.

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.

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.

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.