Invitrogen™ ERO1L Recombinant Superclonal™ Antibody

Descripción

This antibody is predicted to react with Monkey, Pig, and Bovine. Recombinant rabbit Superclonal™ antibodies are unique offerings from Thermo Fisher Scientific. They are comprised of a selection of multiple different recombinant monoclonal antibodies, providing the best of both worlds - the sensitivity of polyclonal antibodies with the specificity of monoclonal antibodies - all delivered with the consistency only found in a recombinant antibody. While functionally the same as a polyclonal antibody - recognizing multiple epitope sites on the target and producing higher detection sensitivity for low abundance targets - a recombinant rabbit Superclonal™ antibody has a known mixture of light and heavy chains. The exact population can be produced in every lot, circumventing the biological variability typically associated with polyclonal antibody production. Note: Formerly called Recombinant polyclonal antibody, this product is now rebranded as Recombinant Superclonal™ antibody. The physical product and the performance remain unchanged.

ERO1L (endoplasmic oxidoreductin-1-like protein) is localized in ER membrane as peripheral membrane protein on the lumenal side. Its association with ERP44 is essential for its retention in the ER and is unique in coupling oxygen reduction to de novo disulfides formation. The ERO1L enzyme is broadly distributed at low levels in several tissues with highest levels in the upper digestive tract and is stimulated by hypoxia via HIF-signaling. ERO1L generally exists as monomer, but has the ability to function as monomer or homodimer and interacts with PDILT. After translation, ERO1L gets n-glycosylated and the disulfide bonds constitute the redox-active center whereby the Cys-94/Cys-99 disulfide bond accepts an electron from P4HB followed by funneling the same to the active site disulfide Cys-394/Cys-397. ERO1L acts by oxidizing directly to P4HB/PDI isomerase through direct disulfide exchange and associates with ERP44. ERO1L is implicated in immunoglobulin folding, oxidative stress, release of unfolded cholera toxin from reduced P4HB/PDI upon Vibrio cholerae infection, and plays a key role in ER stress-induced CHOP-dependent apoptosis through inositol 1,4,5-trisphosphate receptor IP3R1 activation.