Protein Disulfide Isomerase Family A, Member 3 (PDIA3) antibody

Antigen: Protein Disulfide Isomerase Family A, Member 3 (PDIA3)

Synonyms: P58, ER60, ERp57, ERp60, ERp61, GRP57, GRP58, PI-PLC, HsT17083, grp-58, DKFZp468H1910

Clonality: Monoclonal (Map-ERP57)

Host: Mouse

Reactivity: Human, Mouse (Murine), Cow (Bovine), Dog (Canine), Guinea Pig, Hamster, Monkey, Pig (Porcine), Rabbit, Rat (Rattus)

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC)

Catalog no.: ABIN361814

Additional Information

Alternative name: Erp57 (Grp58)

Gene ID: 2923

UniProt: P30101

Immunogen: Human Recombinant Erp57 (Grp58)

Isotype: IgG1

Clone: Map-ERP57

Description: 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-glucosylated 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. 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.

Synonyms: ERp60, ERp61, Grp57, Grp58, P58, PDIA3, PI PLC

Characteristics: Accession Number: NP_005304.3

Specificity: Detects ~57kDa

Sensitivity: 0.5 µg/mL of SMC-168 was sufficient for detection of ERp57 in 10µg of heat shock Heal Lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Application Details

Application Notes: 1:2000 (WB)

Concentration: 1mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.4, 50% glycerol

Storage: Store at -20° C. Shipping Conditions: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins

Restrictions: For Research Use only

Images

Erp57 Western Blotting 1 in 1000 Hu copy.

Publications

Oliver, van der Wal, Bulleid et al.: "Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins." in: Science (New York, N.Y.), Vol. 275, Issue 5296, pp. 86-8, 1997 (PubMed).

Tan, Kropshofer, Mandelboim et al.: "Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 168, Issue 4, pp. 1950-60, 2002 (PubMed).

Chen, Gharib, Huang et al.: "Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 8, Issue 7, pp. 2298-305, 2002 (PubMed).

Kimura, Imaishi, Hagiwara et al.: "ERp57 binds competitively to protein disulfide isomerase and calreticulin." in: Biochemical and biophysical research communications, Vol. 331, Issue 1, pp. 224-30, 2005 (PubMed).

Soldua, Garbi, Haemmerling et al.: "Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle." in: The Journal of biological chemistry, Vol. 281, Issue 10, pp. 6219-26, 2006 (PubMed).

Williams: "Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum." in: Journal of cell science, Vol. 119, Issue Pt 4, pp. 615-23, 2006 (PubMed).

Maattanen, Kozlov, Gehring et al.: "ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations." in: Biochemistry and cell biology = Biochimie et biologie cellulaire, Vol. 84, Issue 6, pp. 881-9, 2007 (PubMed).

Hebert, Molinari: "In and out of the ER: protein folding, quality control, degradation, and related human diseases." in: Physiological reviews, Vol. 87, Issue 4, pp. 1377-408, 2007 (PubMed).

Leclercq, Lardet, Martin et al.: "The green fluorescent protein as an efficient selection marker for Agrobacterium tumefaciens-mediated transformation in Hevea brasiliensis (Müll. Arg)." in: Plant cell reports, Vol. 29, Issue 5, pp. 513-22, 2010 (PubMed).