Peptidi

Peptide H-LLIIGASTR^-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.

Chymostatin is a protein that inhibits the polymerase chain reaction (PCR) by binding to the DNA polymerase. It has been shown to have a hypoglycemic effect in mice with myocardial infarcts and can also induce apoptosis in inflammatory lesions. Chymostatin binds to intracellular targets, such as cell factor and pro-apoptotic protein, which are involved in energy metabolism and inflammatory lesion. The inhibition of these targets may be due to its chemical biology properties, which include the formation of disulfide bonds and basic proteins. Chymostatin is not active against bacterial cells but can inhibit enzyme activities in mammalian cells.

Suc-Ala-Glu-Pro-Phe-pNA is a peptide that is a specific interaction with neutrophils. It is an endogenous factor that has been shown to activate neutrophil functions, such as chemotaxis and phagocytosis. The substrate proteins of this peptide are involved in the regulation of neutrophil functions. Suc-Ala-Glu-Pro-Phe-pNA has also been shown to inhibit the activity of phosphatases, which may lead to inhibition of cell proliferation. The structure activity relationship studies for this peptide show that it can be used as an inhibitor for cells in early stages of development.

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 (231-245) is an epitope candidate with various predicted HLA restrictions. This epitope can be used to better vaccine design for more durable CD4+ and CD8+ T cell responses for long-lasting immunity.

Z-Arg-Arg-AMC hydrochloride salt is a versatile compound that acts as a catalyst and forms strong hydrogen bonds. It exhibits proteolytic activity and has been found to be effective in breaking down proteins. In addition, Z-Arg-Arg-AMC hydrochloride salt has been shown to possess neuroprotective properties, making it a potential candidate for the treatment of neurological disorders. It also demonstrates anthelmintic activity, which means it can be used to combat parasitic worm infections. Furthermore, this compound has antioxidant activity and can help reduce lipid peroxidation, protecting cells from oxidative damage. With its diverse range of characteristics, Z-Arg-Arg-AMC hydrochloride salt holds great promise in various research fields such as biochemistry and medicine.

Peptide derived from the HIV transactivator of transcription protein. TAT is a cationic cell-penetrating peptide.

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

Portion of Influenza NP

H-Thr-AMC is a small molecule that binds to the ubiquitin-proteasome system and inhibits the degradation of proteins. It has been shown to inhibit methionine aminopeptidase, which is an enzyme that degrades amino acids in the intestine. H-Thr-AMC also has a metal chelator effect, which prevents it from being degraded by proteases. The sequence of H-Thr-AMC was derived by sequencing cDNA from eukaryotes. H-Thr-AMC is not active against aminopeptidase A, but can inhibit aminopeptidase B and C. H-Thr-AMC has been shown to have inhibitory effects on both intestinal and physiological properties.br>br>
H-Thr-AMC is a substrate for the peptide:hydrolase (peptidase) family of enzymes known as aminopeptid

Z-Gly-Pro-AMC is a substrate molecule that mimics the natural substrate of dipeptidyl peptidase IV (DPP-IV) and is used in the study of plant physiology. It has been shown to inhibit DPP-IV activity by binding to the enzyme’s active site, preventing it from cleaving biologically active peptides. This drug also has an antidiabetic effect, which may be due to its ability to inhibit α-amylase activity. Z-Gly-Pro-AMC also has been shown to increase locomotor activity and reduce body weight in rats with metabolic disorders. Z-Gly-Pro-AMC inhibits serine proteases, such as trypsin, chymotrypsin, elastase, and cathepsin G, which are involved in tumor progression.

Ac-Lys-pNA hydrochloride is a protease that belongs to the endopeptidase class of proteolytic enzymes. It is used in research and recombinant expression to cleave proteins at specific sites. Ac-Lys-pNA hydrochloride is activated by ammonium sulfate, which binds to the active site of the enzyme. The enzyme also cleaves peptides with Lys or Arg at the C terminus. Ac-Lys-pNA hydrochloride has been shown to be effective against aeruginosa, but not escherichia coli, which are both gram negative bacteria.

Jelleines are a family of very small (8-9 amino acid residues long) host defence peptides (HDPs) isolated from the royal jelly of honey bees (Apis mellifera). Jelleines do not present any similarity with other HDPs from other honeybees and are produced by the workers and secreted into Royal Jelly (RJ), providing abroad-spectrum protection of the bee hive against microbial infections. The Jelleines are not considered cytolytic or directly involved with inflammatory effects. Jelleine-II may be a product of a tryptic digestion of MRJP-1, which is produced in the hypopharyngeal glands of the worker honeybee and secreted into the RJ- an exoproteinase action either on N-or on C-terminal positions of the tryptic fragment could result in the formation of the Jelleines-I and -IV, respectively. Possess antimicrobial properties against yeast, fungi, gram-positive and gram-negative bacteria.PLEASE NOTE that in several published articles the sequence of Jelleine-2 has been printed as TPFKISLHL-NH2-NH2, due to a mistake in the original reference: Fontana et al., (2004). The correct sequence, is TPFKISIHL-NH2.

This peptide is phosphorylated by Janus kinase 2 and 3 (JAK2 and JAK3) and is an ideal substrate for use in kinase assays. The JAK family of kinases is essential for the signalling of a host of immune modulators in tumour, stromal, and immune cells where they are highly expressed. JAK family proteins mediate the signalling of the interferon (IFN), IL-6, and IL-2 families of cytokines.JAK kinases are associated with cytokine receptors. Cytokine binding to these receptors results in activation of JAK kinases and receptor phosphorylation. Phosphorylated cytokine receptors recruit STAT proteins, which are then phosphorylated by the activated JAK kinases. Phosphorylated STAT proteins form homo- and hetero-dimers that translocate into the nucleus and function as transcription factors.This peptide contains an N-terminal biotin tag for easy detection and purification.

ANP (9-22) is derived from the atrial natriuretic peptide (ANP) which is a cardiac hormone involved in maintaining cardio-renal homeostasis. This occurs through the activation of the guanylyl cyclase-coupled receptor, resulting in the increased concentration of cyclic guanylate monophosphate. Moreover its function in the processes of anti-proliferation and anti-angiogenesis allow it to take part in the cardiovascular remodelling process.ANP is a member of the natriuretic peptide family and it is encoded by the NPPA gene, located on chromosome 1. Once synthesized from the 151 amino acid pre-prohormone into its biologically active form, ANP is secreted by the atrial cardiomyocytes in the circulating forms: ANP (1-98) and ANP (99-126). This synthesis process involves the signal peptide being removed from the pre-prohormone resulting in proANP (1-126) which is converted into the circulating forms by the type II transmembrane serine protease Corin.

Portion of EBV

Fragment of the angiotensin-converting enzyme 2 (ACE2) peptidase domain (PD) alpha1 helix, a domain important for the interaction of ACE2 with the severe acute respiratory syndrome (SARS coronavirus receptor binding domain (SARS-CoV-2-RBD). SBP1 associates with the SARS-CoV-2-RBD with nanomolar affinity and can potentially block the key mechanism by which SARS CoV-2 initiates entry into human cells.This peptide has a covalently bonded N-terminal Biotin tag that can be used for detection and purification and contains a polyethylene glycol spacer (PEG4).

(Asp-Glu-Val-Asp)2-Rh110 is a peptide substrate for caspase 3 and 7. It has been shown to be an effective inhibitor of peptidyl prolyl cis, trans isomerase (PPIase) in vitro and in vivo, which may lead to a possible therapeutic target for the treatment of neurodegenerative disorders.

BCL6 encodes a transcription factor that represses genes necessary for the terminal differentiation of lymphocytes within germinal centers, and the misregulated expression of this factor is strongly implicated in several types of B cell lymphoma. The homodimeric BTB domain of BCL6 (also known as the POZ domain) is required for the repression activity of the protein and interacts directly with the SMRT and N-CoR corepressors that are found within large multiprotein histone deacetylase-containing complexes.

Tetanus Toxin P30 (947-967) is a protein that is derived from the single-chain polypeptide neurotoxin produced by Clostridium tetani. The neurotoxins produced by Clostridium tetani are among the most potent molecules known to humankind. Once in the body, the toxin binds to the basal lamina at the neuromuscular junction. From here, the toxin is transported to inhibitory interneurons in the spinal cord, where it prevents the release of neurotransmitters, which causes spastic paralysis.