Recombinant Cricetulus griseus Endoplasmic reticulum chaperone BiP (HSPA5) (Active), Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus), Mammalian cell, C-terminal 10xHis-tagged, 71.8 kDa, purity >95% as determined by SDS-PAGE.

Recombinant Cricetulus griseus Endoplasmic reticulum chaperone BiP (HSPA5) (Active)

Recombinant Cricetulus griseus Endoplasmic reticulum chaperone BiP (HSPA5) (Active) — Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Purity >95%.

SKU: BCACP-000549 Category:
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Product SKUBCACP-000549
Product DescriptionRecombinant Cricetulus barabensis griseus Endoplasmic reticulum chaperone BiP (HSPA5) protein is expressed from Mammalian cell with C-terminal 10xHis-tagged. It contains 19-654aa. [Accession | G3I8R9].
Uniprot No.G3I8R9
Gene NamesHSPA5
PurityGreater than 95% as determined by SDS-PAGE.
Expression SystemMammalian cell
Expression Region19-654aa
SpeciesCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Tag InfoC-terminal 10xHis-tagged
Molecular weight71.8 kDa
ActivityMeasured by its binding ability in a functional ELISA. Immobilized Human FGFR2 at 2 μg/mL can bind Anti-FGFR2 recombinant antibody . The EC50 is 2.051-2.322 ng/mL.
BufferLyophilized from a 0.2 μm filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Alternative NamesEndoplasmic reticulum chaperone BiP; EC:3.6.4.10; 8 kDa glucose-regulated protein; Binding-immunoglobulin protein; Heat shock protein 70 family protein 5; Heat shock protein family A member 5; Immunoglobulin heavy chain-binding protein ; HSPA5; GRP78; I79_019946

Function

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR).

Product Specifications

Recombinant Cricetulus griseus Endoplasmic reticulum chaperone BiP (HSPA5) (Active) is a recombinant protein, expressed in Mammalian cell, covering amino acids 19-654aa, with C-terminal 10xHis-tagged tag, molecular weight 71.8 kDa, purity Greater than 95% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Measured by its binding ability in a functional ELISA. Immobilized Human FGFR2 at 2 μg/mL can bind Anti-FGFR2 recombinant antibody . The EC50 is 2.051-2.322 ng/mL.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

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Protein Biology

Function

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:29198525, PubMed:30710085). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (PubMed:29198525). Also binds and inactivates EIF2AK3/PERK in unstressed cells (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1 and EIF2AK3/PERK, allowing their homodimerization and subsequent activation (PubMed:29198525). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity)

Gene: HSPA5  |  Organism: Cricetulus griseus

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Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

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