BLMH Human

BLM Hydrolase Human Recombinant
Cat. No.
BT26895
Source
Escherichia Coli.
Synonyms

BMH, BH, BLM hydrolase.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

BLMH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 475 amino acids (1-455a.a.) and having a molecular mass of 54.7kDa.
BLMH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Bleomycin hydrolase (BLMH) is a member of the papain superfamily of cysteine proteases and belongs to the peptidase C1 family. Typically found as a homohexamer, BLMH is a cytoplasmic cysteine peptidase. While its standard physiological function remains to be fully elucidated, BLMH is known to confer protection to both normal and cancerous cells against the cytotoxic effects of the glycopeptide antitumor drug bleomycin (BLM). BLMH accomplishes this by catalyzing the inactivation of BLM through hydrolysis of the carboxyamide bond within its β-aminoalaninamide moiety. Notably, BLMH also exhibits broader aminopeptidase activity.
Description
Recombinant BLMH, expressed in E. coli, is produced as a single, non-glycosylated polypeptide chain comprising 475 amino acids (residues 1-455). With a molecular weight of 54.7 kDa, the protein features a 20 amino acid His-tag fused at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Sterile, clear solution.
Formulation
BLMH is supplied as a 1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol.
Purity
The purity of BLMH is determined to be greater than 90% by SDS-PAGE analysis.
Stability
For short-term storage (2-4 weeks), BLMH should be kept at 4°C. For extended storage, it is recommended to store the protein at -20°C. Repeated freeze-thaw cycles should be avoided.
Biological Activity
The specific activity of BLMH is greater than 1,000 pmol/min/µg, as assessed by the hydrolysis of the substrate Met-AMC at pH 7.5 and 37°C.
Synonyms

BMH, BH, BLM hydrolase.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ HVFQHAVPQE GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS YLFFWDKVER CYFFLSAFVD TAQRKEPEDG RLVQFLLMNP ANDGGQWDML VNIVEKYGVI PKKCFPESYT TEATRRMNDI LNHKMREFCI RLRNLVHSGA TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF GVSLKNMNKA ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE DHGHKGYLCM TDEWFSEYVY EVVVDRKHVP EEVLAVLEQE PIILPAWDPM GALAE

Product Science Overview

Structure and Function

BLM Hydrolase is a member of the cysteine protease papain superfamily and contains the signature active site residues characteristic of this family. The enzyme catalyzes the hydrolysis of the carboxamide bond of the B-aminoalaninamide moiety in bleomycin, thereby inactivating the drug. This activity protects both normal and malignant cells from the cytotoxic effects of bleomycin .

Physiological Role

The normal physiological role of BLM Hydrolase remains largely unknown. However, its ability to inactivate bleomycin suggests a protective function against the potential toxicity of this chemotherapeutic agent. This protective role is particularly significant given the dose-dependent pulmonary toxicity associated with bleomycin, which can lead to lung fibrosis and other severe side effects .

Clinical Relevance

BLM Hydrolase has garnered attention for its potential role in bleomycin resistance observed in some tumors. By inactivating bleomycin, the enzyme may contribute to the reduced efficacy of the drug in certain cancer treatments. Understanding the mechanisms of BLM Hydrolase activity and its regulation could provide insights into overcoming drug resistance and improving the therapeutic outcomes of bleomycin-based chemotherapy .

Recombinant BLM Hydrolase

Recombinant BLM Hydrolase refers to the enzyme produced through recombinant DNA technology, which allows for the expression of the human enzyme in various host systems. This recombinant form is used in research to study the enzyme’s structure, function, and potential applications in overcoming bleomycin resistance. The availability of human recombinant BLM Hydrolase facilitates detailed biochemical and pharmacological studies, which are crucial for developing strategies to mitigate the side effects of bleomycin and enhance its therapeutic efficacy .

Research and Development

Ongoing research aims to explore the structure-activity relationship of BLM Hydrolase and its interaction with bleomycin. Efforts are also being made to develop novel bleomycin analogues with improved antitumor activity and reduced toxicity. These studies are essential for advancing our understanding of BLM Hydrolase and its role in cancer therapy .

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Source
<p><span lang="EN-US">Escherichia Coli.</span></p>
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