Specific activity > 20 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of insulin in the presence of DTT.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
PDIA3
Purity
>95%, by SDS-PAGE
Applications/Dilutions
Dilutions
Enzyme Activity
SDS-Page
Theoretical MW
58.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
20 mM Tris-HCl buffer (pH8.0), 1 mM DTT, 0.1 M NaCl, and 10% glycerol
Preservative
No Preservative
Concentration
1 mg/ml
Purity
>95%, by SDS-PAGE
Alternate Names for Recombinant Human ERp57/PDIA3 His Protein
Disulfide isomerase ER-60
EC 5.3.4.1
endoplasmic reticulum P58
Endoplasmic reticulum resident protein 57
Endoplasmic reticulum resident protein 60
ER protein 60
ER60
ERp57
ERp5758 kDa glucose-regulated protein
ERp60
ERp6058 kDa microsomal protein
ERp61
glucose regulated protein, 58kDa
GRP57
GRP58
GRP58ER protein 57
HsT17083
P58
PDIA3
phospholipase C-alpha
PI-PLC
protein disulfide isomerase family A, member 3
protein disulfide isomerase-associated 3
protein disulfide-isomerase A3
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-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 (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).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.
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