|Application ||WB, IHC-P, IF, E|
|Other Accession||P06761, P20029, Q90593, Q0VCX2, Q7SZD3|
|Predicted||Bovine, Chicken, Mouse, Rat|
|Calculated MW||72333 Da|
|Antigen Region||261-289 aa|
|Other Names||78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78|
|Target/Specificity||This HSPA5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 261-289 amino acids from the Central region of human HSPA5.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSPA5 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.|
|Cellular Location||Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
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.
Zhao, C., et al. J. Med. Virol. 82(1):14-22(2010) Zhuang, L., et al. Mod. Pathol. 23(1):45-53(2010) Arnaudeau, S., et al. Proteomics 9(23):5316-5327(2009)
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