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Recombinant Human BAG family molecular chaperone regulator 4 (BAG4)

ACP20662

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP20662 Target NameBAG4
Target SynonymsBAG 4; BAG family molecular chaperone regulator 4; BAG-4; BAG4; BAG4_HUMAN; Bcl 2 associated athanogene 4; Bcl-2-associated athanogene 4; BCL2 associated athanogene 4; Silencer of death domains; SODDFormLyophilized powder
Expression SystemCustom Production. Please inquire and provide the desire expression system.Expression Range1-457
Protein LengthFull length proteinPurity>85% (SDS-PAGE)
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDO95429
Background Information
  • Uniprot Id

    O95429

  • Target Species

    Human

  • Target Name

    BAG4

  • Target Full Name

    BAG family molecular chaperone regulator 4

  • Target Function

    Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Prevents constitutive TNFRSF1A signaling. Negative regulator of PRKN translocation to damaged mitochondria.

  • Target Subcellular Location

    Cytoplasm.

  • Target Tissue Specificity

    Ubiquitous.

  • Target Synonyms

    BAG 4; BAG family molecular chaperone regulator 4; BAG-4; BAG4; BAG4_HUMAN; Bcl 2 associated athanogene 4; Bcl-2-associated athanogene 4; BCL2 associated athanogene 4; Silencer of death domains; SODD

  • Target Background

    The protein encoded by this gene is a member of the BAG1-related protein family. BAG1 is an anti-apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. This protein contains a BAG domain near the C-terminus, which could bind and inhibit the chaperone activity of Hsc70/Hsp70. This protein was found to be associated with the death domain of tumor necrosis factor receptor type 1 (TNF-R1) and death receptor-3 (DR3), and thereby negatively regulates downstream cell death signaling. The regulatory role of this protein in cell death was demonstrated in epithelial cells which undergo apoptosis while integrin mediated matrix contacts are lost. Alternatively spliced transcript variants encoding distinct isoforms have been identified.

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