Mouse anti-Human BIP/GRP78 Monoclonal Antibody | anti-BIP/GRP78 antibody

BIP/GRP78 Mouse mAb

Cat. Num. AAA8538611

• Gene Names: HSPA5; BIP; MIF2; GRP78; HEL-S-89n
• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry, Immunocytochemistry, Flow Cytometry, Functional Assay, ELISA
• Purity: Ascitic Fluid
• Synonyms: BIP/GRP78; Monoclonal Antibody; BIP/GRP78 Mouse mAb; BIP; MIF2; GRP78; FLJ26106; HSPA5; anti-BIP/GRP78 antibody

• Host: Mouse
• Reactivity: Human
• Clonality: Monoclonal
• Isotype: IgG1
• Clone Number: 3B4-H11-C9
• Purity/Purification: Ascitic Fluid
• Form/Format: Ascitic fluid containing 0.03% Sodium Azide.
• Sequence Length: 654

• Applicable Applications for anti-BIP/GRP78 antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Flow Cytometry (FC/FACS), 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.
• Cellular Localization: Cytoplasm, Endoplasmic Reticulum
• Preparation and Storage: Store at 4 degree C short term. Store at -20 degree C long term. Avoid freeze/thaw cycle.

Related Product Information for anti-BIP/GRP78 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. For this reason, BiP has been identified as a marker for various disease states that are associated with secretory and transmembrane protein misfolding.

NCBI and Uniprot Product Information

• NCBI GI #: 16507237
• NCBI GeneID: 3309
• NCBI Accession #: NP_005338.1
• NCBI GenBank Nucleotide #: NP_005338.1
• UniProt Accession #: P11021
• 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: 78 kDa glucose-regulated protein
• UniProt Gene Name: HSPA5
• UniProt Synonym Gene Names: GRP78; GRP-78; BiP
• UniProt Entry Name: GRP78_HUMAN

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

GRP78: a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.

Protein type: Heat shock protein; Chaperone

Chromosomal Location of Human Ortholog: 9q33.3

Cellular Component: signalosome; endoplasmic reticulum membrane; cell surface; focal adhesion; smooth endoplasmic reticulum; mitochondrion; endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; membrane; melanosome; plasma membrane; integral to endoplasmic reticulum membrane; midbody; nucleus

Molecular Function: protein domain specific binding; protein binding; enzyme binding; ubiquitin protein ligase binding; chaperone binding; ATPase activity; unfolded protein binding; ribosome binding; misfolded protein binding; calcium ion binding; glycoprotein binding; ATP binding

Biological Process: platelet activation; ER-associated protein catabolic process; cerebellum structural organization; unfolded protein response; cerebellar Purkinje cell layer development; cellular response to glucose starvation; platelet degranulation; substantia nigra development; unfolded protein response, activation of signaling protein activity; cellular protein metabolic process; positive regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; blood coagulation; ER overload response; positive regulation of cell migration; negative regulation of apoptosis