Description
PDIA3 Antibody | 61-599 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: N/A
Immunogen: This PDIA3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 446-475 amino acids from the C-terminal region of human PDIA3.
Research Area: Signal Transduction
Tested Application: WB, IHC-P, Flow
Application: For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:50~100
For FACS starting dilution is: 1:10~50
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 57 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: Protein disulfide-isomerase A3, 58 kDa glucose-regulated protein, 58 kDa microsomal protein, p58, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 57, ER protein 57, ERp57, Endoplasmic reticulum resident protein 60, ER protein 60, ERp60, PDIA3, ERP57, ERP60, GRP58
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: PDIA3 is 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.