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Erp57 (Grp58) Antibody (OASE00105)

OASE00105
Aviva Systems Biology
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry
Product group Antibodies
TargetPDIA3
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Overview

  • Supplier
    Aviva Systems Biology
  • Product Name
    Erp57 (Grp58) Antibody (OASE00105)
  • Delivery Days Customer
    23
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    Map.ERp57
  • Concentration
    1 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID2923
  • Target name
    PDIA3
  • Target description
    protein disulfide isomerase family A member 3
  • Target synonyms
    ER60, ERp57, ERp60, ERp61, GRP57, GRP58, HEL-S-269, HEL-S-93n, HsT17083, P58, PI-PLC, protein disulfide-isomerase A3, 58 kDa glucose-regulated protein, 58 kDa microsomal protein, ER protein 57, ER protein 60, disulfide isomerase ER-60, endoplasmic reticulum P58, endoplasmic reticulum resident protein 57, endoplasmic reticulum resident protein 60, epididymis secretory protein Li 269, epididymis secretory sperm binding protein Li 93n, glucose regulated protein, 58kDa, phospholipase C-alpha, protein disulfide isomerase-associated 3
  • Host
    Mouse
  • Isotype
    IgG1
  • Scientific 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-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).
  • Storage Instruction
    -20°C
  • UNSPSC
    12352203