GRP78 (HSPA5) Mouse Monoclonal Antibody [Clone ID: 4E3]

Specifications

Product Data
Clone Name	4E3
Applications	ELISA, IHC, WB
Recommend Dilution	Western Blot: 1/500 - 1/2000. Immunohistochemistry on paraffin sections: 1/200 - 1/1000. ELISA: 1/10000.
Reactivity	Human
Host	Mouse
Clonality	Monoclonal
Immunogen	Purified recombinant fragment of human HSPA5 expressed in E. Coli.
Specificity	This antibody reacts to HSPA5.
Formulation	State: Ascites State: Ascitic fluid containing 0.03% sodium azide.
Conjugation	Unconjugated
Storage Condition	Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing.
Predicted Protein Size	78 kDa
Gene Name	heat shock protein family A (Hsp70) member 5
Database Link	Entrez Gene 3309 Human UniProt ID P11021
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.
Synonyms	78 kDa glucose-regulated protein, Heat shock 70 kDa protein 5, BiP
Reference Data

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