InnoPep Inc. products

This 5-amino acid peptide is a sortase substrate, C-terminal sorting signal. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine and the amino group of cell-wall crossbridges. Sortases are a family of Gram-positive transpeptidases responsible for anchoring surface protein virulence factors to the peptidoglycan cell wall layer. Cleavage of this FRET substrate by sortase reveals the fluorescent signal, Abs/Em = 340/490 nm.

This 12 amino acids peptide is a hyaluronan inhibitor (HA), a high molecular weight glycosaminoglycan expressed abundantly in the extracellular matrix and on cell surfaces. This peptide shows specific binding to soluble, immobilized, and cell-associated forms of HA, and it inhibits leukocyte adhesion to HA substrates almost completely.

Rat adrenomedullin, rADM, (1-50) and its C-terminal rADM (11-50) induce a dose-dependent and endothelium-independent vasodilation on the arterial mesenteric vasculature.

This is a tyrosine phosphorylated angiotensin II peptide with a substrate sequence specificity for chymase to act. This is an octapeptide hormone that is formed as a result of the action of human heart chymase, a chymotrypsin-like serine protease on the Phe-His bond of Angiotensin I. The ideal susbtrate for human heart chymase should contain this peptide sequence, and has been demonstrated that the Pro-Phe sequence in P2-P1 positions of peptide substrates is highly favored by leukocyte chymotrypsin-like proteinases such as chymases and cathepsin G.

This is a type I signal peptidase (SPase1) substrate peptide labeled with EDANS/ DABCYL FRET pair, and contains a crucial cleavage site derived from the C-terminal region of the Staphylococcus epidermidis pre-SceD protein. Abs/Em = 340/490 nm.

This peptide is Histone H3 amino acid residues 15-36 with a C-terminal GG linker followed by a biotinylated lysine.

This peptide is derived from fibrinopeptide B amino acid residues 1-14. It is used as a mass spec (MS) standard in proteomic research.