Cell Signaling Technology

Product Pathways - Translational Control

Ero1-Lα Antibody #3264

Applications Reactivity MW (kDa) Source
W H 60 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Ero1-Lα Antibody detects endogenous levels of total Ero1-Lα protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) derived from the sequence around Leu218 of human Ero1-Lα. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using Ero1-Lα Antibody.

Background

Secretory proteins translocate into the endoplasmic reticulum (ER) 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 (1). This process is called oxidative protein folding. Several oxidoreductases of the protein disulfide isomerase (PDI) family essential for disulfide formation and isomerization are localized to the ER (2). Studies have found that the ER-residing protein endoplasmic oxidoreductin-1 (Ero1) provides the oxidizing potential to the ER in Saccharomyces cerevisiae (3). In vitro experiments demonstrated that Ero1 is oxidized by molecular oxygen in a FAD-dependent manner and the oxidized Ero1 in turn serves as an oxidant for PDI (4). Two human homologs of Ero1, Ero1-like (Ero1-Lα and β) have been identified (2,5). Ero1-Lα is an ER membrane-associated N-glycoprotein that promotes oxidative protein folding and has been shown to be expressed in several cell lines and tissues (2).

  1. Huppa, J.B. and Ploegh, H.L. (1998) Cell 92, 145-148.
  2. Cabibbo, A. et al. (2000) J. Biol. Chem. 275, 4827-4833.
  3. Frand, A.R. and Kaiser, C.A. (1998) Mol. Cell 1, 161-170.
  4. Tu, B.P. et al. (2000) Science 290, 1571-1574.
  5. Pagani, M. et al. (2000) J. Biol. Chem. 275, 23685-23692.

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