Polyclonal Anti-PDIA3

Rabbit IgG polyclonal antibody for Protein disulfide-isomerase A3 (PDIA3) detection. Tested with WB, IHC-P in Human;Mouse;Rat. \n

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SPECIFICATIONS

Price

200.00 USD

Catalog Number

PA1679

Size

100ug/vial

Applications

IHC, WB

Reactivities

Hum, Mouse, Rat

Form

Lyophilized

Format

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.

Gene Id

PDIA3

References

1.Bourdi, M., Demady, D., Martin, J. L., Jabbour, S. K., Martin, B. M., George, J. W., Pohl, L. R. cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase. Arch. Biochem. Biophys. 323: 397-403, 1995.\n2.Ellerman, D. A., Myles, D. G., Primakoff, P. A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev. Cell 10: 831-837, 2006\n3.Garbi, N., Tanaka, S., Momburg, F., Hammerling, G. J. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nature Immun. 7: 93-102, 2006.\n

Swiss Prot

P30101

Storage Temp

At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing.

Additional Info

A synthetic peptide corresponding to a sequence in the middle region of human PDIA3, identical to the related rat and mouse sequences.

Scientific Background

PDIA3(Protein disulfide isomerase family A, member 3), also called GRP58, Erp57 or ER60, is an isomerase enzyme, mapped on 15q15.3. The PDIA3 protein has protein disulfide isomerase activity. PDIA3 is also part of the major histocompatibility complex (MHC) class I peptide-loading complex, which is essential for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface. Koivunen et al. showed that PDIA3 could not substitute for the beta subunit of PDI. When coexpressed with alpha prolyl 4-hydroxylase, PDIA3 did not form prolyl 4-hydroxylase tetramers, nor did it have prolyl 4-hydroxylase activity. Hirano et al. expressed human PDIA3 and found that the protein had a thiol-dependent reductase activity. They showed that the expression level of PDIA3 is increased after oncogenic transformation of normal rat kidney cells and NIH 3T3 cells.