Cat: IPD-X23106

Recombinant Mouse BID Protein,His & GST

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Analytical Data

  • Gene name

    BID

  • 简介

    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.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by its binding ability in a functional ELISA. Immobilized mouse BID at 10 μg/mL (100 μL/well) can bind biotinylated human BCL2L1. The ED50 for this effect is 40.75 ng/mL. Measured by its binding ability in a functional ELISA. Immobilized mouse BID at 10μg/mL (100μl/well) can bind biotinylated human BCL2L1,The ED50 for this effect is 40.75 ng/mL.

  • Alternative Names

    BH3-interacting domain death agonist; BID; p15 BID

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His;N-GST

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    EDK99650.1

  • Expression Region

    M12-D206

  • Protein Length

    Partial

  • Molecular Weight

    48 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

The research on BID (BH3-interacting domain death agonist) recombinant protein stems from its critical role in apoptosis regulation and cellular stress response. BID is a pro-apoptotic member of the Bcl-2 family of proteins, which plays a pivotal role in the intrinsic pathway of apoptosis. Upon activation, BID is cleaved to form a truncated form known as tBID, which translocates to the mitochondria and facilitates the release of cytochrome c, ultimately leading to cell death. Understanding the mechanisms by which BID and its derivatives operate is essential for elucidating how cells balance survival and death in physiological and pathological conditions, including cancer, neurodegeneration, and ischemic injury. Researchers have increasingly focused on the recombinant expression of BID and tBID to study their structure-function relationships, binding affinities with other apoptotic regulators, and potential therapeutic applications. By generating and characterizing BID recombinant proteins, scientists aim to develop novel strategies for manipulating apoptosis in cancer therapies, promoting cell survival in neurodegenerative diseases, and enhancing protective mechanisms against cellular damage. The intricate interplay between BID and other apoptotic mediators highlights its significance as a target in drug design and provides valuable insights into the development of more effective treatment regimens aimed at diseases characterized by dysregulated apoptosis.

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