Rabbit Glucose Regulated Protein 94 Polyclonal Antibody | anti-HSP90B1 antibody

Glucose Regulated Protein 94 (Grp94, gp96)

Cat. Num. AAA621692

• Gene Names: HSP90B1; ECGP; GP96; TRA1; GRP94
• Reactivity: Human, Mouse, Rat
• Applications: ELISA, Western Blot, Immunoprecipitation, Immunohistochemistry
• Purity: Purified; Purified by immunoaffinity chromatography.
• Synonyms: Glucose Regulated Protein 94; Polyclonal Antibody; Glucose Regulated Protein 94 (Grp94; gp96); Anti -Glucose Regulated Protein 94 (Grp94; anti-HSP90B1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Specificity: Recognizes mouse, rat and human gp96 proteins. Reactivity has been confirmed with mouse and rat brain homogenates by Western Blot and immunoprecipitation, and with formalin-fixed, paraffin-embedded (FFPE) human tonsil tissue by immunohistochemistry.
• Purity/Purification: Purified; Purified by immunoaffinity chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.4, 0.05% sodium azide.

• Applicable Applications for anti-HSP90B1 antibody: ELISA (EL/EIA), Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC)
• Application Notes: Suitable for use in ELISA, Western Blot, Immunoprecipitation and Immunohistochemistry.; Dilution: ELISA: 0.1-1ug/ml; Western Blot: 1-3ug/ml. Identifies a single band at ~96kD; Immunoprecipitation: 1-5ug/ml; Immunohistochemistry: 0.5-1ug/ml Heat induced epitope retrieval (HIER) with EDTA, pH 8.0, is required prior to staining for formalin-fixed, paraffin-embedded (FFPE) tissues.
• Immunogen: Synthetic peptide derived from the N-terminal region of the mouse and human gp96 protein. Species Sequence Homology: Pig, cow, and dog : 100%
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for anti-HSP90B1 antibody

The tumor rejection antigen (gp96), also known as glucose-regulated protein 94 (GRP94), is a member of the heat shock protein (HSP) family. The gp96 protein is up-regulated by stress conditions such as glucose starvation and heat shock, and its function is regulated through a ligand-dependent conversion from an active to an inactive conformation. gp96 is involved in both innate and adaptive immunity. A study has shown that a B-cell line deficient in gp96 is unresponsive to microbial stimuli because toll-like receptors (TLRs) are retained intracellularly. However, normal surface levels of TLRs were restored when these cells were transfected with a cDNA encoding gp96. The tumor rejection antigen can activate the release of nitric oxide by antigen presenting cells (APCs) and it also has a relevant role in the regulation of immune responses to pathological cell death.

Product Categories/Family for anti-HSP90B1 antibody

Antibodies; Abs to Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 553324
• NCBI GeneID: 7184
• UniProt Accession #: P14625; Q96A97; Q59FC6; Q5CAQ5; Q96GW1
• Molecular Weight: 92,469 Da
• NCBI Official Full Name: glucose regulated protein 94
• NCBI Official Synonym Full Names: heat shock protein 90kDa beta (Grp94), member 1
• NCBI Official Symbol: HSP90B1
• NCBI Official Synonym Symbols: ECGP; GP96; TRA1; GRP94
• NCBI Protein Information: endoplasmin; GRP-94; gp96 homolog; tumor rejection antigen 1; 94 kDa glucose-regulated protein; Tumor rejection antigen-1 (gp96); tumor rejection antigen (gp96) 1; glucose regulated protein, 94 kDa; endothelial cell (HBMEC) glycoprotein; heat shock protein 90 kDa beta member 1
• UniProt Protein Name: Endoplasmin
• Protein Family: Endoplasmin
• UniProt Gene Name: HSP90B1
• UniProt Synonym Gene Names: GRP94; TRA1
• UniProt Entry Name: ENPL_HUMAN

NCBI Description

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]

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

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

Cellular Component: extracellular matrix; endoplasmic reticulum membrane; focal adhesion; membrane; perinuclear region of cytoplasm; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome; plasma membrane; extracellular region; midbody; cytosol; 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; ER-associated protein catabolic process; protein transport; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; unfolded protein response; sequestering of calcium ion; response to hypoxia; toll-like receptor signaling pathway; innate immune response; regulation of phosphoprotein phosphatase activity; negative regulation of apoptosis