Meprin A Beta (MEP1b)

PPH Beta; Endopeptidase-2; Meprin B; PABA Peptide Hydrolase; N-benzoyl-L-tyrosyl-P-amino-Benzoic Acid Hydrolase Subunit Beta

Meprin A Beta (MEP1b)
Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes and in leukocytes and certain cancer cells. Mature meprins are oligomers of evolutionarily related, separately encoded alpha and/or beta subunits. Homooligomers of meprin-alpha (MEP1A) are secreted; oligomers containing meprin-beta are associated with the plasma membrane.
Mep1b-null mice were born at half the expected mendelian ratio, but those that survived developed normally and were viable and fertile. Mutant mice lacked membrane-associated Mep1a in kidney and intestine, and microarray analysis indicated that renal gene expression profiles were different than those of wildtype mice.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)