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Bleomycin hydrolase (BMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution\; however, the only known activity of the enzyme is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. Additionally we are shipping BLMH Proteins (23) and BLMH Kits (12) and many more products for this protein.
Showing 10 out of 87 products:
Human Monoclonal BLMH Primary Antibody for WB - ABIN396175
Sowa, Bennett, Gygi, Harper: Defining the human deubiquitinating enzyme interaction landscape. in Cell 2009
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Human Polyclonal BLMH Primary Antibody for WB - ABIN1881112
Ferrando, Velasco, Campo, Lopez-Otin: Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. in Cancer research 1996
Show all 3 references for ABIN1881112
Human Polyclonal BLMH Primary Antibody for WB - ABIN1881113
Brömme, Rossi, Smeekens, Anderson, Payan: Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization. in Biochemistry 1996
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Human Polyclonal BLMH Primary Antibody for ELISA, WB - ABIN560067
Englert, Kliment, Ramsgaard, Milutinovic, Crum, Tobolewski, Oury: Paradoxical function for the receptor for advanced glycation end products in mouse models of pulmonary fibrosis. in International journal of clinical and experimental pathology 2011
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Chicken Polyclonal BLMH Primary Antibody for WB - ABIN2786515
de Haas, Zwart, Meijer, Nuver, Boezen, Suurmeijer, Hoekstra, van der Steege, Sleijfer, Gietema: Variation in bleomycin hydrolase gene is associated with reduced survival after chemotherapy for testicular germ cell cancer. in Journal of clinical oncology : official journal of the American Society of Clinical Oncology 2008
Blmh interacts with diverse cellular processes--lipoprotein, amino acid and protein, carbohydrate, and energy metabolisms, detoxification, antioxidant defenses--that are essential for normal kidney homeostasis.
Bleomycin hydrolase protects against neurodegeneration associated with elevated homocysteine thiolactone levels in hyperhomocysteinemia and Alzheimer's disease.
bleomycin hydrolase functions as an MHC class I epitope-processing protease
BH does not play a major role either in generating or destroying class I major histocompatibility antigen (MHC)-presented peptides that bind to the MHC in living cells. These results point to redundant functions between peptidases.
Bleomycin hydrolase downregulation in lesional skin of adult atopic dermatitis patients is independent of filaggrin (show FLG Antibodies) gene mutations
This study findings suggest that Blmh interacts with diverse cellular processes from energy metabolism and anti-oxidative defenses to cell cycle, cytoskeleton dynamics, and synaptic plasticity essential for normal brain homeostasis.
We also detected significant association between XRCC1 (show XRCC1 Antibodies), XRCC3 (show XRCC3 Antibodies), and BLHX polymorphisms and a high frequency of chromosomal damage
The caspase (show CASP3 Antibodies)-dependent cleavage of BLH was confirmed by cleavage of partly-purified human bleomycin hydrolase with caspase-3 (show CASP3 Antibodies).
present study suggests that our new method can detect novel genes of interest and that BLMH is a suppressor gene in HCC (show FAM126A Antibodies)
This first report on BLMH carrier status in Tunisia shows o association between carrying the BLMH-G genotype and Alzheimer's disease in epsilon4 negative or positive subjects.
Cysteine proteases bleomycin hydrolase and cathepsin Z (show CTSZ Antibodies) mediate N-terminal proteolysis and toxicity of mutant huntingtin (show HTT Antibodies).
BH activity and expression were markedly decreased in AD lesional skin, suggesting a defect of the filaggrin (show FLG Antibodies) degradation pathway in AD.
The homozygous variant G/G of BLMH gene SNP A1450G is associated with reduced survival and higher prevalence of early relapses in TC patients treated with bleomycin-containing chemotherapy.
Bleomycin hydrolase (BMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution\; however, the only known activity of the enzyme is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. The protein contains the signature active site residues of the cysteine protease papain superfamily.
, bleomycin hydrolase
, BLM hydrolase
, aminopeptidase H