Peptídeos

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

Ac-Pro-Arg-Asn-Lys-Acc-NH2 is a peptide that is used to study the catalytic mechanism of enzymes. It has been shown to be an effective substrate for tryptase, which is an enzyme that plays a role in the degradation of proteins. Ac-Pro-Arg-Asn-Lys-Acc-NH2 binds to the active site of tryptase and undergoes a series of reactions that lead to its hydrolysis. The rate constants for these reactions have been measured in order to determine kinetic constants.

Peptide LCBiot-EDQVDPRLIDG-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.

H-Val-Lys-Gly-Ile-Leu-Ser-NH2 is a biologically active peptide. It is a peptide that is derived from the amino acid sequence of protease activated receptor 2 (PAR2) and has been shown to induce coagulation. This peptide has also been shown to have cardiovascular effects, such as reducing blood pressure, and may be useful in the treatment of hypertension.

Fmoc-Val-Wang Resin (100-200 mesh) 1% DVB is a resin that is used in the synthesis of peptides. The resin contains Fmoc-protected amino acids, which are cleaved by the use of hydrogen fluoride to release the free acid form. This resin is characterized by its high purity and low viscosity. It has been shown to be an excellent building block for peptide synthesis, as well as a useful tool for biological studies.

Vasopressin is a peptide antidiuretic hormone, originating from the hypothalamus, that regulates water balance in the body. It is also known as arginine vasopressin or antidiuretic hormone (ADH). The clinical efficacy of vasopressin has been evaluated using in vitro methods on mouse monoclonal antibody production cells, blood sampling, and microdialysis probes for monitoring blood pressure. This product is available in the salt form: Acetate.

Feleucin-B01 was recently identified from the skin secretion of the toad Bombina orientalis with a role in preventing the host from bacterial infection. Synthetic feleucin-B01 shows limited antimicrobial activity against a reference Gram-positive bacterium and is ineffective against the Gram-negative and yeast strains. The mode of action of the non-apeptide is lysis of the bacterial membrane resulting in rapid bacterial death. Feleucin-B01 shows a limited role in the secreted host defences which is complemented by the range of alternate antimicrobial peptides (AMP) also excreted. The amphipathic feleucin-B01 sequence is being studied as a template to hopefully generate more potent synthetic versions with a broader range of activity.

Please enquire for more information about (Pyr 3)-Amyloid β-protein (3-42) including the price, delivery time and more detailed product information at the technical inquiry form on this page

Cytomegalovirus (CMV) is a prevalent human pathogen of concern in the immunocompromised such as during organ transplant or in AIDs patients- it can potentially be fatal. Due to the commonness of CMV, one strategy being developed is prevention of viral reactivation in immunosuppressed groups. Current antivirals have significant toxicity thus pushing the search for a specific CMV therapy.Murine CMV has been well established as a model for human CMV, including its susceptibility to T cell mediated clearance. The immediate-early protein 1 (IE1) was fragmented and used to find the best IE1 epitope as a vaccine. YPHFMPTNL, provided here, recognized by H-2 Ld-restricted CD8+ T cells was the best epitope of IE1 for T cell recognition. The fragment has been used to successfully generate CD8+ T cell clones specific for the IE1 epitope of murine CMV. This peptide has the potential to further the development of antiviral immunotherapy for CMV and better understand its ability to evade the host immunity.

Alloferon 2, a member of the Alloferons was extracted from the blood of a Callifora vicina fly who had been experimentally infected. The Alloferons are, bioactive, cationic peptides and can stimulate Natural Killer cell activity and IFN synthesis.

Anti-microbial peptide (AMP) designed using only residues G, L, and K (GLK-19). Active against-Escherichia coli-with higher activity relative to human AMP LL-37 and also weakly active against methicillin-resistant Staphylococcus aureus (MRSA), but not-active against HIV-1. Activity against E. coli with a minimal inhibitory concentration (MIC) at 10 mM.

The Insulysin FRET substrate [Mca]/[Dnp] is a synthetic insulysin peptide substrate that contains an N-terminal fluorescent 7-methoxycoumarin (Mca) group and a C-terminal 2, 4-dinitrophenyl (Dnp) quencher. 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.Insulysin, also known as insulin-degrading enzyme (IDE), is a highly conserved zinc metallopeptidase that contains an inverted zincin motif (HXXEH), characteristic of the inverzincin family of proteases. Insulysin functions as a dimer and exhibits allosteric kinetics, whereby small substrate peptides and polyphosphates such as ATP can act as enzyme activators. The endopeptidase cleaves a wide variety of substrates that are diverse in length, structure and sequence and exhibits a preference for basic or bulky hydrophobic residues.Insulysin is ubiquitously expressed and is responsible for insulin catabolism and the degradation of many bioactive peptide substrates including glucagon, TGF-alpha, β-endorphin, dynorphins and atrial natriuretic peptide. Insulysin also selectively degrades amylin and β-amyloid amyloidogenic peptides at multiple sites.Fluorescence Resonance Energy Transfer (FRET) peptides are convenient tools for the study of peptidase specificity and enzymatic activity.

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 (250-264) is a class I (Kb)-restricted peptide epitope of OVA. The ovalbumin fragment is presented by the class I MHC molecule, H-2Kb.

Fluorogenic substrate peptide to assay trypsin-like activity. In its intact state this peptide is non-fluorescent, however when the Rhodamine fluorophore is released upon hydrolysation, fluorescence can be detected. This peptide is therefore a useful tool for analysing trypsin-like enzyme activity.The presence of the D-proline residue on the C terminal of the rhodamine molecule ensures one directional rhodamine cleavage which simplifies fluorescence studies. Rhodamine 110 is a laser grade fluorescent dye with excitation maxima at 496 nm and emission maxima at 522 nm.

Protease activated receptors (PARs) are a distinctive four-member family of seven transmembrane G protein-coupled receptors (GPCRs) widely expressed in inflammatory cells. PARs are cleaved by certain serine proteases to expose a tethered ligand domain, this ligand domain then binds to and activates the receptors to initiate multiple signalling cascades. These PAR-activating proteases therefore represent PAR agonists. This PAR-3 agonist peptide represents the sequence of the 'tethered ligand' and is therefore capable of activating the receptor independently of N-terminal proteolysis.PAR-3 is required for intercellular adhesion molecule 1 (ICAM-1) expression in endothelial cells and PAR-3 cooperates with PAR-1 to mediate the effect of thrombin on cytokine production and vascular cell adhesion molecule (VCAM- 1) expression.

Histone H3 (1 - 20) 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. 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. Like 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 many lysine and arginine residues, they have a positive net charge which interacts electrostatically 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 alter the positioning of the nucleosome, allowing the DNA to be either available or inaccessible to the transcription machinery.Histone tails can undergo multiple modifications, including acetylation, methylation, ubiquitylation and sumoylation.  The purpose of the modifications is believed to alter chromatin function/structure.  Histone H3 (1 - 20), with no modifications, is a valuable peptide in the study of epigenetics. It can aid in understanding interaction with histone effectors and the histone tail using crystallisation and pull-down assays on affinity matrices. Histone H3 (1 - 20)  is labelled with the Aurora Fluor 647 fluorescent tag.

Macropin-1 (MAC-1) is an anti-microbial peptide (AMP) isolated from venom of the solitary bee Macropis fulvipes (Hymenoptera: Melittidae). MAC-1 has activity against both Gram-positive and Gram-negative bacteria, including drug-resistant strains. MAC-1 can inhibit biofilm formation in Staphylococcus aureus and Pseudomonas aeruginosa and also exhibits anti-fungal activity. MAC-1 has little to no haemolytic activity against human cells at microbiologically effective concentrations.Macropin acts by first binding to negatively charged bacterial membrane components- such as peptidoglycan (PTG) or lipopolysaccharide (LPS). Macropin then kills the bacteria by disrupting the outer bacterial membrane and depolarising the cytoplasmic membrane to cause cell penetration.