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

In Stock
Code: CSB-MP6869DXU
Size:
20ug
20ug100ug1mg
US$190
Quantity:
Express system: Mammalian cell
Species: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Tag Info: C-terminal 10xHis-tagged
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Product Details

Abbreviation
Recombinant Cricetulus griseus HSPA5 protein (Active)
Purity
Greater than 95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU/ug as determined by LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized Cricetulus griseus HSPA5 at 2 μg/mL can bind Anti-HSPA5 recombinant antibody (CSB-RA010827MA1HU). The EC50 is 1.884-2.205 ng/mL.
Target Names
HSPA5
Uniprot NO.
Alternative Names
Endoplasmic 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
Species
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Source
Mammalian cell
Expression Region
19-654aa
Target Protein Sequence
EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTSEKDEL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
71.8 kDa
Protein Length
Full Length of Mature Protein
Tag Info
C-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Buffer
Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4
Storage
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Lead Time
3-7 business days
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Shelf Life
The shelf life is related to many factors, storage state, storage temperature and the stability of the product itself. Generally, the shelf life of lyophilized form is 6 months at -20°C/-80°C from the date of receipt.
Troubleshooting and FAQs
Datasheet & COA
Please contact us to get it.
Images
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Activity
    Measured by its binding ability in a functional ELISA. Immobilized Cricetulus griseus HSPA5 at 2 μg/ml can bind Anti-HSPA5 recombinant antibody (CSB-RA010827MA1HU). The EC50 is 1.884-2.205 ng/mL.
Description

BiP (HSPA5) orchestrates protein folding quality control in the endoplasmic reticulum and translocates to the cell surface in stressed or malignant cells, making it a pivotal target in cancer biology and unfolded protein response research. This full-length mature protein (aa 19–654) demonstrates quantifiable binding activity with an EC50 of 1.884–2.205 ng/mL against anti-HSPA5 antibody in functional ELISA, providing a validated reagent for antibody-antigen interaction studies, inhibitor screening campaigns, and IC50 determination assays targeting BiP-client protein interfaces. The C-terminal 10×His tag preserves the N-terminal ATPase domain and substrate-binding pocket, supporting use in enzymatic activity assays that measure ATP hydrolysis rates and in kinetic parameter analysis to define Km and kcat values for chaperone-substrate interactions. Endotoxin levels below 1.0 EU/μg and purity exceeding 95% meet the stringent criteria required for cell-based assays investigating ER stress pathways and for serving as a positive control in enzyme-linked functional screens.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
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 ERN1/IRE1-mediated unfolded protein response (UPR). 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. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. 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.
Gene References into Functions
  1. These findings suggest a molecular mechanism by which AMPylation serves as a switch to inactivate BiP, limiting its interactions with substrates whilst conserving ATP. PMID:29064368
  2. BiP inactivation by AMPylation of its SBD does not disturb Hsp70 inter-domain allostery and preserves BiP structure. Instead it relies on a redistribution of the BiP conformational ensemble and stabilization the domain-docked conformation in presence of ADP and ATP. PMID:29064369

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Subcellular Location
Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface.
Protein Families
Heat shock protein 70 family
Database Links
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No. 269, Shendun 5th Road, Donghu Hi-Tech Development Area, Hubei Province, 430206, P.R.China
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