GRP78 antibody

Catalog No. ABIN969204

This anti-GRP78 antibody is a Mouse Monoclonal antibody detecting GRP78 in WB, ELISA and IHC. Suitable for Human. This Primary Antibody has been cited in 3+ publications.

Quick Overview for GRP78 antibody (ABIN969204)

Target: GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This GRP78 antibody is un-conjugated

Application: Western Blotting (WB), ELISA, Immunohistochemistry (IHC)

Clone: 4E3

Product Details anti-GRP78 Antibody

Purpose: HSPA5 Antibody

Purification: Ascitic fluid

Immunogen: Purified recombinant fragment of human HSPA5 expressed in E. Coli.

Isotype: IgG1

Application Details

Application Notes: ELISA: 1/10000

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Ascitic fluid containing 0.03 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: 4 °C,-20 °C

Storage Comment: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.

References for anti-GRP78 antibody (ABIN969204)

Tanimoto, Sakaguchi, Abarzua, Kataoka, Kurose, Murata, Nasu, Kumon, Huh: "Down-regulation of BiP/GRP78 sensitizes resistant prostate cancer cells to gene-therapeutic overexpression of REIC/Dkk-3." in: International journal of cancer. Journal international du cancer, Vol. 126, Issue 7, pp. 1562-9, (2010) (PubMed).

Zhuang, Scolyer, Murali, McCarthy, Zhang, Thompson, Hersey: "Lactate dehydrogenase 5 expression in melanoma increases with disease progression and is associated with expression of Bcl-XL and Mcl-1, but not Bcl-2 proteins." in: Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, Vol. 23, Issue 1, pp. 45-53, (2010) (PubMed).

Honda, Horie, Daito, Ikuta, Tomonaga: "Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface." in: Journal of virology, Vol. 83, Issue 23, pp. 12622-5, (2009) (PubMed).

Target Details for GRP78

Target: GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))

Alternative Name: HSPA5

Background: When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) (PubMed 8020977) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell.Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.The HSP70 proteins are ubiquitous molecular chaparones that are found in all organisms and tissue types. Like other members of the HSP70 family, BiP is a peptide-binding ATPase that is able to differentiate native proteins from unfolded polypeptides. BiP does not bind to fully folded and assembled proteins, except in the presence of other co-chaparones. BiP is involved in a number of key mechanisms and pathways including polypeptide translocation across the endoplasmic reticulum, folding, assembly, transport of secreted or membrane proteins, and the regulation of calcium homeostasis. Although BiP is relatively abundant, marked increases in BiP occur where there is an accumulation of unfolded polypeptides. For this reason, BiP has been identified as a marker for various disease states that are associated with secretory and transmembrane protein misfolding.

Molecular Weight: 78 kDa

UniProt: P11021

Pathways: Thyroid Hormone Synthesis, ER-Nucleus Signaling