Rat GRP94 Monoclonal Antibody | anti-HSP90B1 antibody

GRP94 Antibody: HRP

Cat. Num. AAA801937

• Reactivity: Human, Mouse, Rat, Bovine, Canine, Chicken, Guinea pig, Hamster, Horse, Monkey, Pig, Rabbit, Sheep, Xenopus
• Applications: Western Blot, Immunoprecipitation, Flow Cytometry, Functional Assay
• Synonyms: GRP94; Monoclonal Antibody; GRP94 Antibody: HRP; HSP90B1; GP96; TRA1; ECGP; anti-HSP90B1 antibody

• Host: Rat
• Reactivity: Human, Mouse, Rat, Bovine, Canine, Chicken, Guinea pig, Hamster, Horse, Monkey, Pig, Rabbit, Sheep, Xenopus
• Clonality: Monoclonal
• Isotype: IgG2a
• Clone Number: 9G10
• Form/Format: Protein G Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 803

• Applicable Applications for anti-HSP90B1 antibody: Western Blot (WB), Immunoprecipitation (IP), Flow Cytometry (FC/FACS)
• Application Notes: 0.5ug/ml was sufficient for detection of Grp94 in 20ug of HeLa lysate.
• Conjugate: HRP
• Storage Buffer: PBS pH7.2, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Western Blot (WB)

(Western Blot analysis of Human Cervical cancer cell line (HeLa) lysate showing detection of GRP94 protein using Rat Anti-GRP94 Monoclonal Antibody, Clone 9G10. Primary Antibody: Rat Anti-GRP94 Monoclonal Antibody at 1:1000. Secondary Antibody: HRP Goat Anti-Rat.)

Related Product Information for anti-HSP90B1 antibody

Background Info: Detects a 98kDa protein corresponding to the molecular mass of Grp94 on SDS PAGE immunoblots. Does not detect human Hsp90, Grp74, or GrpE from E.coli.

Scientific Background: Grp94 (glucose regulated protein 94, gp96) is a constitutively expressed endoplasmic reticulum (ER) lumenal protein that is up-regulated in response to cellular stress such as heat shock, oxidative stress or glucose depletion. Grp94 is thought to play a role in protein translocation to the ER, in their subsequent folding and assembly, and in regulating protein secretion (1). Grp94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific CTL responses to chaperone bound peptides via MHC class I pathway (2) Grp94 is a member of the Hsp90 family of stress proteins and shares sequence homology with its cytosolic equivalent, Hsp90 (3). Both Hsp90 and Grp94 are calcium binding proteins (4). Despite sharing 50% sequence homology over its N domains and complete conservation in its ligand binding domains with Hsp90, Grp94 and Hsp90 differ in their interactions with regulatory ligands as Grp94 has weak ATP binding and hydrolysis activity (5). Grp94 exists as a homodimer and the two subunits interact at two distinct intermolecular sites, C terminal dimerization domains and the N-terminal interacts with the middle domain of opposing subunits. (6). Grp94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER (7).

Product Categories/Family for anti-HSP90B1 antibody

Chaperones; Heat Shock; Trafficking

References

1. Rudolph R.W., and Bedows E. (1997) J Biol Chem 272: 3125-3128. 2. Srivastava P.K., et al. (1994) Immunogenetics. 39(2):93- 98. 3. Mazzarella R.A., and Green M. (1987) J Biol Chem 262: 8875-8883. 4. Kang, H.S. and Welch W.J. (1991) J Biol Chem 266(9): 5643-5649. 5. Soldano K.L., et al. (2003) J Biol Chem 278(48): 48330- 48338. 6. Chu F., et al. (2006) Protein Sci 15(6): 1260-1269. 7. Peter F., et al., (1992) J Biol Chem 267: 10631-10637. 8. Allen S. et al. (2000) Blood 96(2): 560-568. 9. Sato K et al. (2001) Blood 98(6): 1852-1857. 10. Yun S.-W. et al (2000) Brain Research Bulletin.52(5): 371-378. 11. Choukhi A., et al. (1998) J. Virol. 72: 3851-3858. 12. Hoshino T., et al. (1998) Blood 91(11): 4379-4386. 13. Riera M. et al. (1999) Mol. Cell Biochem. 191: 97-104. 14. Gusarova V., et al. (2001) J. Biol. Chem. 276(27): 24891- 24900.

NCBI and Uniprot Product Information

• NCBI GI #: 4507677
• NCBI GeneID: 7184
• NCBI Accession #: NP_003290.1
• NCBI GenBank Nucleotide #: NM_003299.2
• UniProt Accession #: P14625; Q96A97
• Molecular Weight: 92,469 Da
• NCBI Official Full Name: endoplasmin
• UniProt Protein Name: Endoplasmin
• Protein Family: Endoplasmin
• UniProt Gene Name: HSP90B1
• UniProt Synonym Gene Names: GRP94; TRA1; GRP-94
• UniProt Entry Name: ENPL_HUMAN

NCBI Description

This gene encodes a member of a family of adenosine triphosphate(ATP)-metabolizing molecular chaperones with roles in stabilizing and folding other proteins. The encoded protein is localized to melanosomes and the endoplasmic reticulum. Expression of this protein is associated with a variety of pathogenic states, including tumor formation. There is a microRNA gene located within the 5' exon of this gene. There are pseudogenes for this gene on chromosomes 1 and 15. [provided by RefSeq, Aug 2012]

Uniprot Description

GRP94: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9. Interacts with CNPY3. This interaction is disrupted in the presence of ATP. Interacts with TLR4 and TLR9, but not with TLR3. Belongs to the heat shock protein 90 family.

Protein type: Heat shock protein; Apoptosis; Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 12q24.2-q24.3

Cellular Component: endoplasmic reticulum membrane; focal adhesion; endoplasmic reticulum lumen; endoplasmic reticulum; extracellular region; cytosol; extracellular matrix; membrane; perinuclear region of cytoplasm; plasma membrane; melanosome; midbody; nucleus

Molecular Function: protein binding; low-density lipoprotein receptor binding; RNA binding; unfolded protein binding; virion binding; calcium ion binding; protein phosphatase binding; ATP binding

Biological Process: actin rod formation; receptor-mediated endocytosis; protein transport; ER-associated protein catabolic process; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; unfolded protein response; sequestering of calcium ion; toll-like receptor signaling pathway; response to hypoxia; innate immune response; regulation of phosphoprotein phosphatase activity; negative regulation of apoptosis