ERP44 antibody

Source

Rabbit

Reactivity

Human;Mouse;Rat;Monkey

Background

Secretory proteins translocate into the endoplasmic reticulum after their 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. Disulfide isomerase has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds. Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum resident protein 44, constitute the PDI family. ERp44 is induced upon ER stress and is linked to Ero1-Lα and Ero1-Lβ through mixed disulfide bonds. ERp44 was shown to mediate the ER localization of Ero1-Lα.

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] Anelli, T. et al. (2002) EMBO J 21, 835-44.
[4] Anelli, T. et al. (2003) EMBO J 22, 5015-22.

Raw materials

Preparation Products