Bioactivity | Histatin-3, a 32 amino acid peptide, possesses powerful antimicrobial properties. Histatin-3 behaves as a substrate for proprotein convertase 1 (PC1), being cleaved by this endoprotease primarily at a site carboxy terminal to the single Arg25 residue (HRGYR decrease SN). Histatin-3 is a moderately potent, reversible and competitive inhibitor of the furin-mediated cleavage of the pentapeptide pGlu-Arg-Thr-Lys-Arg-MCA fluorogenic substrate, with an estimated inhibition constant Ki of 1.98 μM[1]. |
Name | Histatin-3 |
CAS | 112844-49-2 |
Sequence | Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg-Ser-Asn-Tyr-Leu-Tyr-Asp-Asn |
Shortening | DSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN |
Formula | C178H258N64O48 |
Molar Mass | 4062.35 |
Transport | Room temperature in continental US; may vary elsewhere. |
Storage | Please store the product under the recommended conditions in the Certificate of Analysis. |
Reference | [1]. A Basak, et al. Histidine-rich human salivary peptides are inhibitors of proprotein convertases furin and PC7 but act as substrates for PC1. J Pept Res. 1997 Jun;49(6):596-603. |