|Datasheet||Specific References||Reviews||Related Products||Protocols|
|NME1, AWD, GAAD, NB, NBS, NDPK-A, NDPKA, NM23, NM23-H1|
|A DNA sequence encoding the human BLMH (NP_000377.1) (Ser 2-Glu 455) was expressed, with a polyhistide tag at the N-terminus.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 88 % as determined by SDS-PAGE|
|Measured by its ability to hydrolyze Met-AMC . The specific activity is >500 pmoles/min/μg.|
|Please contact us for more information.|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human BLMH consisting of 461 amino acids and has a calculated molecular mass of 53.4 kDa as estimated in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile PBS, pH 7.4|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
The papain superfamily member bleomycin hydrolase (BLMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution. 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 papain superfamily member bleomycin hydrolase (BLMH) is a neutral cysteine protease with structural similarity to a 20S proteasome. Bleomycin (BLM), a clinically used glycopeptide anticancer agent. BLMH is an essential protectant against BLM-induced death and has an important role in neonatal survival and in maintaining epidermal integrity. Sequencing revealed several putative sites phosphorylated by different types of protein kinases, but no signal sequence, transmembrane domain, N-linked glycosylation site or DNA-binding motif.