Mouse HSPA5/BIP protein (Recombinant) (N-His) (STJP009346)

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STJP009346
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Mouse HSPA5/BIP-N-His protein was developed from e. coli and has a target region of N-His. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: Hspa5
Gene ID: 14828
Uniprot ID: BIP_MOUSE
Immunogen Region: Met1-Leu654
Immunogen: Mus musculus (Mouse)
Post Translational Modifications In unstressed cells, AMPylation at Thr-519 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins. In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity.
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). 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. Also binds and inactivates EIF2AK3/PERK in unstressed cells. 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. 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.
Protein Name Endoplasmic Reticulum Chaperone Bip
78 Kda Glucose-Regulated Protein
Grp-78
Binding-Immunoglobulin Protein
Bip
Heat Shock Protein 70 Family Protein 5
Hsp70 Family Protein 5
Heat Shock Protein Family A Member 5
Immunoglobulin Heavy Chain-Binding Protein
Database Links Reactome: R-MMU-3371453
Reactome: -MMU-983170
Cellular Localisation Endoplasmic Reticulum Lumen
Melanosome
Cytoplasm
Cell Surface
Identified By Mass Spectrometry In Melanosome Fractions From Stage I To Stage Iv
Localizes To The Cell Surface In Epithelial Cells
High Levels Of Free Iron Promotes Cell Surface Localization
Alternative Protein Names Endoplasmic Reticulum Chaperone Bip protein
78 Kda Glucose-Regulated Protein protein
Grp-78 protein
Binding-Immunoglobulin Protein protein
Bip protein
Heat Shock Protein 70 Family Protein 5 protein
Hsp70 Family Protein 5 protein
Heat Shock Protein Family A Member 5 protein
Immunoglobulin Heavy Chain-Binding Protein protein
Hspa5 protein
Grp78 protein

Information sourced from Uniprot.org