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C106

Recombinant Human BID/BH3-interacting domain death agonist

10ug

640

576

现货

国产

C106

Recombinant Human BID/BH3-interacting domain death agonist

50ug

2000

1800

现货

国产

C106

Recombinant Human BID/BH3-interacting domain death agonist

500ug

12320

11088

现货

国产

C106

Recombinant Human BID/BH3-interacting domain death agonist

1mg

17600

15840

现货

国产

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  • Catalog# C106
    Source E.coli
    Description Recombinant Human BH3-Interacting Domain Death Agonist/BID is produced with our E. coli expression system. The target protein is expressed with sequence (Met1-Asp195) of Human BID protein.
    Names BH3-Interacting Domain Death Agonist, p22 BID, BID
    Accession # P55957
    Formulation Supplied as a 0.2 μm filtered solution of 20mM PB, 100mM KCl, pH 7.4
    Shipping The product is shipped on dry ice/ice packs.
    Storage Store at < -20°C, stable for 6 months after receipt.
    Please minimize freeze-thaw cycles.
    Purity Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
    Endotoxin Less than 0.1 ng/μg (1 IEU/μg).
    Amino Acid Sequence
    MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSS HSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATA LEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD
    Background BH3-Interacting Domain Death Agonist (BID) is a member of the Bcl-2 protein family which regulates outer mitochondrial membrane permeability. BID is a pro-apoptotic member that causes cytochrome c to be released from the mitochondria intermembrane space into the cytosol. Interaction of Bid with Bak causes altered mitochondrial membrane permeability. BID contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. It is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent, and also offer a new strategy for the treatment of acute renal failure associated with ischemia-reperfusion. BID receives direct inputs from a key regulator of the cell cycle arrest/DNA repair machinery (ATM), and therefore is an excellent candidate to coordinate genotoxic stress responses and apoptotic cell death. BID is a novel pro-apoptosis Bcl-2 family protein that is activated by caspase 8 in response to Fas/TNF-R1 death receptor signals. Deletion of BID inhibits carcinogenesis in the liver, although this genetic alteration promotes tumorigenesis in the myeloid cells. This is likely related to the function of BID to promote cell cycle progression into S phase. BID could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint.