Recombinant Golden hamster GRP78 BiP protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Golden hamster GRP78 BiP protein is a Syrian hamster Full Length protein, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE, WB.
View Alternative Names
GRP78, HSPA5, Endoplasmic reticulum chaperone BiP, 78 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, GRP-78, BiP, HSP70 family protein 5
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Golden hamster GRP78 BiP protein (AB92363)
SDS-PAGE Analysis :
Lane 1 : Molecular weight markers
Lane 2 : ab92363 0.5 μg
Lane 3 : ab92363 1 μg
Lane 4 : ab92363 2 μg
Lane 5 : ab92363 5 μg
Complementary Products
Reagents, Controls & Accessories
AB116029
Prestained Protein Ladder - Extra broad molecular weight (5 - 245 kDa)
- 5
- 1
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
GRP78/BiP is important in the unfolded protein response (UPR) a cellular stress response related to the ER. It is part of a complex that manages protein load inside the ER by regulating the fold of nascent proteins and interacting with other ER stress sensors like IRE1 PERK and ATF6. This function is essential for maintaining proper protein conformation in the ER especially during physiological stress ensuring that only correctly folded proteins proceed to the Golgi apparatus.
Pathways
GRP78/BiP significantly affects the UPR and apoptosis pathways. By controlling protein folding and quality in the ER GRP78 helps prevent cell death under stress conditions. It works closely with other proteins like ATF6 which activates stress response genes. In normal conditions GRP78 keeps stress transducers inactivated but during stress it dissociates allowing UPR signaling to occur.
Specifications
Form
Liquid
Additional notes
Purified by Multi-step chromatography.
General info
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). 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 (By similarity). 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).
Sequence similarities
Belongs to the heat shock protein 70 family.
Post-translational modifications
In unstressed cells, AMPylation at Thr-518 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.
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com