Recombinant BID protein (His tag)

Recombinant BID protein (His tag)

Cat.#: 540070

Size:

Special Price 383.1 USD

Availability: 3-4 weeks
- +

Add to cart to get an online quotation

Product Information

  • Product Name
    Recombinant BID protein (His tag)
  • Documents
  • Description

    Recombinant Human BH3-interacting domain death agonist (BID) Fragment (residues 82-195) is a high-purity protein fragment designed for structural and biochemical studies. This 114-amino acid segment includes key functional domains and offers excellent stability and solubility, making it ideal for apoptosis research, caspase activation assays, and mitochondrial signaling investigations.

    BH3-interacting domain death agonist (BID) is a crucial regulator of apoptosis in human cells. The full-length protein induces caspase activation and programmed cell death while countering the protective effects of BCL2. Following cleavage, BID generates active fragments including p15 BID, which translocates to mitochondrial membranes and facilitates cytochrome c release. BID primarily localizes to the cytoplasm in its uncleaved form, with cleaved fragments targeting mitochondrial outer membranes. This protein plays a central role in connecting death receptor signaling to mitochondrial apoptosis pathways, making it essential for understanding cell death mechanisms in both normal physiology and disease states.

  • Protein name
    BH3-interacting domain death agonist
  • Uniprot ID
    P55957
  • Gene Name
    BID
  • Source/Expression Host
    E. coli
  • Expression Plasmid/cDNA
    DNA encoding 82-195 aa (P55957) were fused with 6His tag.
  • Sequence
    82-195
  • Protein Species
    Human
  • Molecular weight
    Predictes a molecular mass of 14.56 kDa. In SDS-PAGE under reducing conditions, it migrates as an approximately 15 kDa band.
  • Purity
    >90%, by SDS-PAGE with Coomassie Brilliant Blue staining.
  • Activity
    Not tested.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"