ERp57 Antibody: ATTO 390

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. ERp57 deletion impairs posttranslational phases of influenza hema-glutinin folding, and causes accelerated release of MHC-I molecules, resulting in the coupling of sub-optimal peptides and reduced expression and stability on the cell surface (6). ERp57 also contains two thioredoxin active-site sequences, CGHC and an estrogen-binding domain. ERp57 is induced by both estrogen and leuteinizing-hormone-releasing hormone in the hippocampus (7).

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A 1:1000 dilution of SMC-266 was sufficient for detection of ERp57 in 15 µg of HeLa by ECL immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary Antibody.

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.