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Results for "

Bid

" in MedChemExpress (MCE) Product Catalog:

8

Inhibitors & Agonists

3

Peptides

3

Recombinant Proteins

1

Antibodies

Cat. No. Compare Product Name Species Source
  • HY-P7662

    rHuBid; BH3-Interacting Domain Death Agonist; Bid

    Human E. coli
    BID Protein, Human expresses in E. coli. The BH3-only protein BID, a pro-apoptotic member of the Bcl-2 family, was initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways.
  • HY-P72852

    BH3-interacting domain death agonist; Bid; p15 Bid

    Mouse E. coli
    BID Protein, a pro-apoptotic member of the Bcl-2 family, is initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. BID Protein, Mouse (His-GST) is the recombinant mouse-derived BID protein, expressed by E. coli , with N-His, N-GST labeled tag. The total length of BID Protein, Mouse (His-GST) is 195 a.a., with molecular weight of ~48 kDa.
  • HY-P701328

    BH3-interacting domain death agonist; Bid; p15 Bid

    Mouse E. coli
    BID Protein, a pro-apoptotic member of the Bcl-2 family, is initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. BID Protein, Mouse (His) is the recombinant mouse-derived BID protein, expressed by E. coli , with C-His labeled tag. The total length of BID Protein, Mouse (His) is 195 a.a., with molecular weight of ~22.72 kDa.

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