Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - Translational Control

ERp72 (D70D12) XP® Rabbit mAb #5033

Applications Reactivity Sensitivity MW (kDa) Isotype
W IF-IC F H M R Mk Endogenous 72 Rabbit IgG

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

* Product-specific protocol.

Specificity / Sensitivity

ERp72 (D70D12) XP® Rabbit mAb detects endogenous levels of total ERp72 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the residues surrounding Met279 of human ERp72 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using ERp72 (D70D12) XP® Rabbit mAb.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of Hep G2 cells using ERp72 (D70D12) XP® Rabbit mAb (blue) compared to a nonspecific negative control antibody (red).

IF-IC

IF-IC

Confocal immunofluorescent analysis of PANC-1 cells using ERp72 (D70D12) XP® Rabbit mAb (green) and β-Actin (8H10D10) Mouse mAb #3700 (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).


Background

Secretory proteins translocate into the endoplasmic reticulum (ER) during synthesis 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) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess thioredoxin homology domains, including ER stress protein 72 (ERp72), constitute the PDI family (3,4). ERp72 contains three thioredoxin homology domains (3) and plays a role in the formation and isomerization of disulfide bonds (3,4).

  1. Huppa, J.B. and Ploegh, H.L. (1998) Cell 92, 145-8.
  2. Ellgaard, L. and Ruddock, L.W. (2005) EMBO Rep 6, 28-32.
  3. Mazzarella, R.A. et al. (1990) J Biol Chem 265, 1094-101.
  4. Satoh, M. et al. (2005) Cell Stress Chaperones 10, 278-84.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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