BLMH Mouse
Escherichia Coli.
BMH, BH, BLM hydrolase, Bleomycin Hydrolase.
Greater than 90.0% as determined by SDS-PAGE.
Description
BLMH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 478 amino acids (1-455 aa) and having a molecular mass of 54.9 kDa.
BLMH is fused to a 23 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
BMH, BH, BLM hydrolase, Bleomycin Hydrolase.
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MGSMNNAGLN SEKVSALIQK LNSDPQFVLA QNVGTTHDLL
DICLRRATVQ GAQHVFQHVV PQEGKPVTNQ KSSGRCWIFS CLNVMRLPFM KKFNIEEFEF
SQSYLFFWDK VERCYFFLNA FVDTAQKKEP EDGRLVQYLL MNPTNDGGQW DMLVNIVEKY
GVVPKKCFPE SHTTEATRRM NDILNHKMRE FCIRLRNLVH SGATKGEISS TQDAMMEEIF
RVVCICLGNP PETFTWEYRD KDKNYHKIGP ITPLQFYKEH VKPLFNMEDK ICFVNDPRPQ
HKYNKLYTVD YLSNMVGGRK TLYNNQPIDF LKKMVAASIK DGEAVWFGCD VGKHFNGKLG
LSDMNVYDHE LVFGVSLKNM NKAERLAFGE SLMTHAMTFT AVSEKDNQEG TFVKWRVENS
WGEDHGHKGY LCMTDEWFSE YVYEVVVDKK HVPEEVLAVL EQEPIVLPAW DPMGALAE
Product Science Overview
The primary biological function of BLMH is to hydrolyze homocysteine thiolactone, a reactive electrophile . Additionally, BLMH plays a significant role in the metabolic inactivation of bleomycin, thereby protecting cells from the cytotoxic effects of this chemotherapeutic agent . This enzyme is a member of the papain superfamily and shares structural similarities with the 20S proteasome .
Recombinant Mouse BLMH is typically produced using E. coli as the expression host . The recombinant protein is often tagged with a His-tag to facilitate purification. The molecular weight of the recombinant protein is approximately 53.3 kDa, although it may appear as 47 kDa on SDS-PAGE due to post-translational modifications .
BLMH contains the signature active site residues of the cysteine protease papain superfamily . It has several putative phosphorylation sites but lacks a signal sequence, transmembrane domain, N-linked glycosylation site, or DNA-binding motif . The enzyme’s activity is measured by its ability to hydrolyze Met-AMC, with a specific activity greater than 500 pmoles/min/μg .
The metabolic inactivation of bleomycin by BLMH is crucial for reducing the cytotoxic effects of this chemotherapeutic agent. BLMH is also essential for neonatal survival and maintaining epidermal integrity . Its role in hydrolyzing homocysteine thiolactone highlights its importance in protecting cells from reactive electrophiles .
