Recombinant Human BLMH/Bleomycin Hydrolase Protein Summary
| Description |
A bioactive recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 1-455 of Human BLMH/Bleomycin Hydrolase Source: E.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 |
| Details of Functionality |
Specific activity: > 2,500 pmole/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of Met-AMC to Methionine and AMC per minute at pH7.5 at 37C. |
| Source |
E. coli |
| Protein/Peptide Type |
Recombinant Protein |
| Gene |
BLMH |
| Purity |
>90%, by SDS-PAGE |
Applications/Dilutions
| Dilutions |
- Bioactivity
- Functional
- SDS-Page
|
| Theoretical MW |
54.7 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
| Buffer |
20 mM Tris-HCl buffer (pH 8.0), 10% glycerol |
| Preservative |
No Preservative |
| Concentration |
1 mg/ml |
| Purity |
>90%, by SDS-PAGE |
Alternate Names for Recombinant Human BLMH/Bleomycin Hydrolase Protein
Background
BLMH is a member of the papain superfamily of the cysteine protease and the peptidase C1 family. It is a cytoplasmic cysteinepeptidase commonly found as a homohexamer. The normal physiological role of BLMH is unknown, but it protects normal and malignant cells from the glycopeptide antitumor drug BLM. It catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and also shows general aminopeptidase activity. Recombinant human BLMH protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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