Recombinant Mouse BLMH Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0417

Recombinant Mouse BLMH Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0417
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Product Overview

Tag His
Host Species Mouse
Accession NP_848760.1
Synonym AI035728, Bh, Bmh
Background 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 2S 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.
Description A DNA sequence encoding the mouse BLMH (NP_848760.1) (Asn 2-Glu 455) was expressed, with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Asn 2-Glu 455
Molecular Weight The recombinant mouse BLMH consisting of 461 a.a. and has a calculated molecular mass of 53.3 kDa. rmBLMH migrates as an approximately 47 kDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Measured by its ability to hydrolyze Met-AMC. The specific activity is >500 pmoles/min/ug.
Formulation Lyophilized from sterile 50mM Tris, 0.15M NaCl, 10% glycerol, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity.
Subcellular Location Cytoplasm. Cytoplasmic granule.
Protein Families Peptidase C1 family
Database References

Gene Functions References

  1. 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. PMID: 24913063
  2. Bleomycin hydrolase protects against neurodegeneration associated with elevated homocysteine thiolactone levels in hyperhomocysteinemia and Alzheimer's disease. PMID: 22227865
  3. bleomycin hydrolase functions as an MHC class I epitope-processing protease PMID: 12140188
  4. 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. PMID: 17513741

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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