|Reactivity||Human Mouse Rat|
|Tested applications||WB IHC IF IP RIP|
|Recommended Dilution||WB 1:500 - 1:2000
IHC 1:50 - 1:200
IF 1:20 - 1:100
IP 1:20 - 1:50
RIP 1:20 - 1:50|
|Observed MW||Refer to Figures|
|Immunogen||Recombinant protein of human P4HB|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
Western blot analysis of extracts of various cell lines, using P4HB antibody.
Immunofluorescence analysis of HeLa cell using P4HB antibody. Blue: DAPI for nuclear staining.
During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).
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