Anti-Meprin A Alpha (MEP1a)

Meprins, members of the 'astacin family' of metalloendopeptidases, are capable of hydrolyzing a variety of peptide and protein substrates. Two forms of meprins, designated A and B, were isolated from the kidney of mice, and both hydrolyzed proteins such as azocasein and insulin B chain. Meprin A (EC 3.4.24.18) is the best characterized of the meprins and is known to hydrolyze peptides such as bradykinin, melanocyte-stimulating hormone, neurotensin, luteinizing hormone releasing hormone, transforming growth factor-alpha, and parathyroid hormone. Meprin B from mouse kidney has latent proteolytic activity against polypeptide substrates. Rat meprin A is sometimes referred to as endopeptidase-2 or endopeptidase-24.18, human meprin A is also called N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA peptide) hydrolase (PPH).

Western blotting: 1:100-400, Immunocytochemistry in formalin fixed cells: 1:100-500, Immunohistochemistry in formalin fixed frozen section: 1:100-500, Immunohistochemistry in paraffin section: 1:50-417

PPHA, PABA Peptide Hydrolase

Mouse