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

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Code CSB-MP6869DXU
Abbreviation Recombinant Cricetulus griseus HSPA5 protein (Active)
MSDS
Size $190
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  • (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. Biological Activity Assay
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Product Details

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
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
Mol. Weight
71.8 kDa
Protein Length
Full Length of Mature Protein
Tag Info
C-terminal 10xHis-tagged
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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 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
Subcellular Location
Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface.
Protein Families
Heat shock protein 70 family
Database Links
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301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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