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Antigenic Specificity | Erp57 (Grp58) |
Clone | [Map.ERP57] |
Host Species | Mouse |
Reactive Species | human, mouse, bovine, dog, guinea pig, hamster, monkey, porcine, rabbit, rat |
Isotype | IgG1 |
Format | unconjugated |
Size | 0.05 mg, 0.2 mg |
Concentration | 1mg/mL |
Applications | Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC) |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | Background Info: Detects ~57kDa Scientific Background: ERp57, also known as Glucose Regulated Protein 58 (Grp58), Hormone-Induced Protein-70 (HIP-70) and microsomal Carnitine Palmitoyltransferase, is a member of the protein disulfide isomerase family, containing two canonical CXHC tetrapeptide active site motifs (1-5). It has quite a few diverse roles. It functions as an accessory oxidoreductase involved in disulfide bond formation. In the ER, ERp57 interacts with membrane bound calnexin and soluble calreticulin (lectin chaperones) via their praline rich P-domain arms. Lectin chaperones bind nascent non-native glycoproteins, and position ERp57 to act upon the immature or misfolded glycoproteins that possess mono-glycosylated side chains. ER |
Immunogen | n/a |
Other Names | [ERp60; ERp61; Grp57; Grp58; P58; PDIA3; PI PLC], [PDIA3; PDIA3; P58; ER60; ERp57; ERp60; ERp61; GRP57; GRP58; PI-PLC; HsT17083; HEL-S-269; HEL-S-93n; ERP57; ERP60; GRP58; p58; ER protein 57; ERp57; ER protein 60; ERp60] |
Gene, Accession # | Gene ID: 2923, NCBI: NP_005304.3, UniProt: P30101 |
Catalog # | MBS801026 |
Price | $250, $405 |
Order / More Info | Erp57 (Grp58) Antibody from MYBIOSOURCE INC. |
Product Specific References | 1. Herbert D.N. and Molinari M. (2007) Physiol Rev. 87: 1377-1408. 2. Williams D.B. (2005) J Cell Sci. 119: 615-623 3. Maattanen P., et al. (2006) Biochem Cell Biol. 84: 881-889. 4. Oliver J.D., et al. (1999) Mol Bio Cell. 10: 2573-2582. 5. Oliver J.D., et al. (1997) Science 275: 86-88. 6. Solda T., et al. (2006) J Biol Chem 281: 6219-6226. 7. Kimura T., et al. (2005) Biochem Biophys Research Communications. 331 (1): 224-230. 8. Chen, G., et al. (2002) Clin Cancer Res 8(7): 2298-2305. 9. Tan, P., et al. F. (2002) J Immunol 168(4): 1950-1960. 1. Lynes, E.M. et al. (2013). Palmitoylation is the Switch that Assigns Calnexin to Quality Control or ER Calcium Signaling. J Cell Sci. Advance Online Article July 10, 2013. doi: 10.1242/jcs.125856 |