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| | ERp72 Antibody Chemical Properties |
| | ERp72 Antibody Usage And Synthesis |
| Source | Rabbit | | Reactivity | Human;Mouse;Rat;Monkey | | Background | Secretory proteins translocate into the endoplasmic reticulum 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. This process is called oxidative protein folding. Protein disulfide isomerase has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds. Other ER resident proteins that possess thioredoxin homology domains, including ER stress protein 72, constitute the PDI family. ERp72 contains three thioredoxin homology domains and plays a role in the formation and isomerization of disulfide bonds. | | References | [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. |
| | ERp72 Antibody Preparation Products And Raw materials |
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