|Calculated MW||54.7 kDa (475 aa, 1-455 aa + NT His Tag)|
|Other Names||Bleomycin hydrolase, BH, BMH.|
|Results||>1,000 pmole/min/ µg|
|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|
|Storage||-80°C; 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteine peptidase usually found as a homohexamer. The standard physiological role of BLMH has not been determined, but it shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.
Ferrando A.A.,et al.Cancer Res. 56:1746-1750(1996).
Broemme D.,et al.Biochemistry 35:6706-6714(1996).
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Totoki Y.,et al.Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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