Mouse anti-Human HSPA5 Antibody | anti-HSPA5 antibody

HSPA5 Antibody

Cat. Num. AAA850996

• Gene Names: HSPA5; BIP; MIF2; GRP78; HEL-S-89n
• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry, ELISA
• Synonyms: HSPA5; HSPA5 Antibody; BIP; MIF2; GRP78; FLJ26106; anti-HSPA5 antibody

• Host: Mouse
• Reactivity: Human
• Isotype: IgG1
• Clone Number: 4E3
• Form/Format: Ascitic fluid containing 0.03% sodium azide.
• Sequence Length: 654

• Applicable Applications for anti-HSPA5 antibody: Western Blot (WB), Immunohistochemistry (IHC), ELISA (EIA)
• Application Notes: WB: 1:500-1:2000; IHC: 1:200-1:1000; ELISA: 1:10000
• Immunogen: Purified recombinant fragment of human HSPA5 expressed in E. Coli.
• Preparation and Storage: Store at 4 degree C, for long term storage, store at-20 degree C.

Western Blot

(Western blot analysis using HSPA5 mouse mAb against NIH/3T3 (1), Hela (2) and Jurkat (3) cell lysate.)

Immunohistochemistry

(Immunohistochemical analysis of paraffinembedded human Thyroid tissues using HSPA5 mouse mAb)

Related Product Information for anti-HSPA5 antibody

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.

Product Categories/Family for anti-HSPA5 antibody

Autophagy antibody; Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells

NCBI and Uniprot Product Information

• NCBI GI #: 16507237
• NCBI GeneID: 3309
• NCBI Accession #: NP_005338.1
• NCBI GenBank Nucleotide #: NM_005347.4
• UniProt Accession #: P11021; Q2EF78; Q9NPF1; Q9UK02; B0QZ61
• Molecular Weight: 78kDa
• NCBI Official Full Name: endoplasmic reticulum chaperone BiP
• NCBI Official Synonym Full Names: heat shock protein family A (Hsp70) member 5
• NCBI Official Symbol: HSPA5
• NCBI Official Synonym Symbols: BIP; MIF2; GRP78; HEL-S-89n
• NCBI Protein Information: endoplasmic reticulum chaperone BiP
• UniProt Protein Name: Endoplasmic reticulum chaperone BiP
• UniProt Gene Name: HSPA5
• UniProt Synonym Gene Names: HSP70 family protein 5Curated

NCBI Description

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.[provided by RefSeq, Sep 2010]

Uniprot Description

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). 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 (). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). 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 (). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 ().