P4HB Rabbit mAb [X2I4]Cat NO.: A28465

Protein names ：P4HB,ERBA2L,PDI,PDIA1,PO4DB,PDIA1_HUMAN,Protein disulfide-isomerase

UniProtID ：P07237

MASS(da) ：57,116

MW(kDa) ：57 kDa

Form ：Liquid

Purification ：Protein A purification

Host ：Rabbit

Isotype ：IgG

sensitivity ：Endogenous

Reactivity ：Human

• ApplicationDilution
• 免疫印迹(WB)1:1000-2000
• 免疫组化(IHC)1:100
• The optimal dilutions should be determined by the end user

Specificity ：Antibody is produced by immunizing animals with a synthetic peptide at the sequence of human P4HB

Storage ：Antibody store in 10 mM PBS, 0.5mg/ml BSA, 50% glycerol. Shipped at 4°C. Store at-20°C or -80°C. Products are valid for one natural year of receipt.Avoid repeated freeze / thaw cycles.

WB Positive detected ： A431 cells

Function ： This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9,the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307)..

Subcellular locationi ：Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome. Cell membrane,Peripheral membrane protein.

IMPORTANT: For western blots, incubate membrane with diluted primary antibody in 1% w/v BSA, 1X TBST at 4°C overnight.