Anti-Glucose Regulated Protein 78 Antibody, Non-Fucosylated (BioBet-1010ZP) (CAT#: BioBet-1010ZP) Datasheet

HSPA5

heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)

The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.

HSPA5; heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); BIP; MIF2; GRP78; HEL-S-89n; 78 kDa glucose-regulated protein; immunoglobulin heavy chain-binding protein; epididymis secretory sperm binding protein Li 89n; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78

Endoplasmic reticulum

Diseases associated with HSPA5 include Mucormycosis and Wolfram Syndrome 1.

Its related pathways are Cellular response to heat stress and Response to elevated platelet cytosolic Ca2+.

UniProtKB/swis-prot reviews the HSPA5 gene endoplasmic reticulum chaperone that plays a key role in endoplasmic reticulum cavity protein folding and quality control. Through the interaction with DNAJC10/ERdj5, it participates in the correct folding of the protein and the degradation of misfolded proteins, which may promote the release of DNAJC10/ERdj5 from its substrate (through similarity). As a key inhibitor of the unfolded protein response (UPR) mediated by ERN1/ire1. In the non-stressed endoplasmic reticulum, DNAJB9/ERdj4 is recruited to the luminal area of ​​ERN1/IRE1, leading to the destruction of the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (similarity). The accumulation of misfolded proteins in the endoplasmic reticulum results in the release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (through similarity). It plays a supporting role in the post-translational transport of small pre-secretory proteins in the endoplasmic reticulum (ER). It can be used as an allosteric modulator to form transposon complexes in the SEC61 channel, and may cooperate with SEC62 to produce these precursors into the SEC61 channel. It seems to specifically regulate the translocation of precursors with inhibitory residues in their mature regions, weakening channel gating. It may also play a role in cell apoptosis and cell proliferation.

Controls and Markers antibody; ER Marker antibody; Endoplasmic reticulum antibody

1.AMPylated by FICD. 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 (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity) 2.Modification sites at PhosphoSitePlus 3.Glycosylation at Thr69, Thr203, and Thr643 4.Ubiquitination at Lys96, Lys113, Lys118, Lys213, Lys268, Lys326, Lys370, Lys376, Lys523, Lys547, Lys573, and Lys601

Protein Based Therapies
Monoclonal antibody (mAb)

IgG

BioBet-1010ZP

Human

Human

The anti-GRP78 antibody that bind specifically to the cell surface of cancer cells, leading to the accomplishment of treatment for cancer.

Cancer

Cancer