Rabbit GRP78 (Bip) Polyclonal Antibody | anti-HSPA5 antibody

GRP78 (Bip) Antibody

Cat. Num. AAA806047

• Gene Names: HSPA5; BIP; MIF2; GRP78; HEL-S-89n
• Reactivity: Human, Mouse, Rat, Canine
• Applications: Western Blot, ELISA, Immunohistochemistry
• Synonyms: GRP78 (Bip); Polyclonal Antibody; GRP78 (Bip) Antibody; BIP; Grp78; HspA5; MIF2; immunoglobulin heavy chain binding protein; anti-HSPA5 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat, Canine
• Clonality: Polyclonal
• Form/Format: Protein A Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 654

• Applicable Applications for anti-HSPA5 antibody: Western Blot (WB), ELISA (EIA), Immunohistochemistry (IHC)
• Application Notes: 1:1000-1:2000 (WB)
• Certificate of Analysis: 0.5 ug/ml of SPC-180 was sufficient for detection of Grp78 in 10ug of rat tissue lysate by ECL immunoblot analysis using goat anti-rabbit IgG:HRP as the secondary antibody.
• Storage Buffer: PBS, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Western Blot (WB)

(Western blot analysis of Human Glucose deprived glia cell lysates showing detection of GRP78 protein using Rabbit Anti-GRP78 Polyclonal Antibody (SPC-180). Primary Antibody: Rabbit Anti-GRP78 Polyclonal Antibody (SPC-180) at 1:1000.)

Related Product Information for anti-HSPA5 antibody

Background Info: Detects a protein with a mass of ~78kDa corresponding to Grp78.

Scientific Background: GRP78 is a ubiquitously expressed, 78-kDa glucose regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia, to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).

Product Categories/Family for anti-HSPA5 antibody

Chaperones; Heat Shock; Organelle Markers; Trafficking

References

1. Cho, S. et al. (2007). Mol Cell Biol 27(1): 368-83. 2. Yang, Y. et al. (1998) J Biol Chem 273: 25552-25555. 3. Luo, S. et al (2006) 26 (15): 5688-97. 4. Yu, Z. et al. (1999) Exp Neurol. 15: 302-314. 5. Koomagi, R. et al. (1999) Anticancer Res. 19:4333- 4336. 6. Laquerre, S. et al. (1998) J. Virology 72: 4940-4949. 7. Dong, D. et al. (2005) Cancer Res 65(13): 5785-91.

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: 72,333 Da
• NCBI Official Full Name: 78 kDa glucose-regulated protein
• NCBI Official Synonym Full Names: heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
• NCBI Official Symbol: HSPA5
• NCBI Official Synonym Symbols: BIP; MIF2; GRP78; HEL-S-89n
• NCBI Protein Information: 78 kDa glucose-regulated protein; immunoglobulin heavy chain-binding protein; epididymis secretory sperm binding protein Li 89n; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
• 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: Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 9q33.3

Cellular Component: signalosome; endoplasmic reticulum membrane; focal adhesion; smooth endoplasmic reticulum; cell surface; mitochondrion; endoplasmic reticulum lumen; endoplasmic reticulum; ER-Golgi intermediate compartment; membrane; plasma membrane; melanosome; 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; calcium ion binding; misfolded protein 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; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; positive regulation of protein ubiquitination; blood coagulation; negative regulation of transforming growth factor beta receptor signaling pathway; ER overload response; positive regulation of cell migration; negative regulation of apoptosis