PDIA3 Antilichaam

This gene encodes a protein of the endoplasmic reticulum that interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. The protein was once thought to be a phospholipase; however, it has been demonstrated that the protein actually has protein disulfide isomerase activity. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. This protein also functions as a molecular chaperone that prevents the formation of protein aggregates.

2923

P30101

Human, Mouse, Rat

Recombinant fusion protein containing a sequence corresponding to amino acids 206-505 of human PDIA3 (NP_005304.3) .

Unconjugated

Primary Antibodies

Apoptosis, Cell Cycle, Signal Transduction

Affinity purification

NIH/3T3

Batch dependent

PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

None

Blue Ice

Store at -20˚ C. Avoid freeze / thaw cycles.

Observed: 57kDa

IgG

PDIA3

MCF7

Jurkat

HepG2

LO2

Mouse brain

Protein disulfide isomerase family A, member 3

Homo sapiens

Protein disulfide isomerase family A, member 3, ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, 58 kDa microsomal protein, endoplasmic reticulum P58, glucose regulated protein, 58 kDa, phospholipase C-alpha, protein disulfide isomerase-associated, ERP57, ERP60

WB, IHC, IF

Liquid