BLMH/Bleomycin Protein, Mouse (P. pastoris, His)

Bleomycin Hydrolase Protein (BLMH) is crucial for cellular defense, inactivating the antitumor drug Bleomycin (BLM) by hydrolyzing its carboxamide bond. This neutralizes BLM's cytotoxic effects, protecting normal and malignant cells. BLMH's exact physiological function is unknown, but its significance in maintaining cellular balance and defending against harmful agents is evident. BLMH/Bleomycin Protein, Mouse (P. pastoris, His) is the recombinant mouse-derived BLMH/Bleomycin protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of BLMH/Bleomycin Protein, Mouse (P. pastoris, His) is 455 a.a., with molecular weight of 53.8 kDa.

BLM hydrolase, also known as Bleomycin hydrolase, plays a crucial role in cellular defense mechanisms by catalyzing the inactivation of the antitumor drug Bleomycin (BLM), a glycopeptide. This enzymatic activity involves the hydrolysis of the carboxamide bond within the B-aminoalaninamide moiety of BLM, leading to its inactivation. This process serves to protect both normal and malignant cells from the toxic effects of BLM. While the precise physiological function of BLM hydrolase remains unclear, its ability to neutralize the cytotoxic impact of BLM highlights its significance in cellular homeostasis and defense against potentially harmful agents.

Mouse

P. pastoris

N-6*His

Q8R016 (M1-E455)

104184  [NCBI]

MNNAGLNSEKVSALIQKLNSDPQFVLAQNVGTTHDLLDICLRRATVQGAQHVFQHVVPQEGKPVTNQKSSGRCWIFSCLNVMRLPFMKKFNIEEFEFSQSYLFFWDKVERCYFFLNAFVDTAQKKEPEDGRLVQYLLMNPTNDGGQWDMLVNIVEKYGVVPKKCFPESHTTEATRRMNDILNHKMREFCIRLRNLVHSGATKGEISSTQDAMMEEIFRVVCICLGNPPETFTWEYRDKDKNYHKIGPITPLQFYKEHVKPLFNMEDKICFVNDPRPQHKYNKLYTVDYLSNMVGGRKTLYNNQPIDFLKKMVAASIKDGEAVWFGCDVGKHFNGKLGLSDMNVYDHELVFGVSLKNMNKAERLAFGESLMTHAMTFTAVSEKDNQEGTFVKWRVENSWGEDHGHKGYLCMTDEWFSEYVYEVVVDKKHVPEEVLAVLEQEPIVLPAWDPMGALAE

53.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.