protein

ERO1L Protein, Human (HEK293, His)

HY-P70893

10 μg;50 μg

155;430 USD

ERO1L Protein, Human (HEK293, His)

proteins

HEK293

10 μg;50 μg

155;430 USD

ERO1L protein is an oxidoreductase that can effectively reoxidize P4HB/PDI in the endoplasmic reticulum and promote the formation of disulfide bonds. It transfers electrons to molecular oxygen, producing reactive oxygen species (ROS). ERO1L Protein, Human (HEK293, His) is the recombinant human-derived ERO1L protein, expressed by HEK293 , with C-6*His labeled tag. The total length of ERO1L Protein, Human (HEK293, His) is 445 a.a., with molecular weight of ~71.0 kDa.

Human

ERO1L protein functions as an oxidoreductase, facilitating disulfide bond formation within the endoplasmic reticulum (ER). Its primary role involves efficiently reoxidizing P4HB/PDI, an enzyme crucial for catalyzing protein disulfide formation, enabling P4HB to engage in successive rounds of disulfide bond formation. Following the reoxidation of P4HB, ERO1L transfers electrons to molecular oxygen through its flavin adenine dinucleotide (FAD) cofactor, leading to the generation of reactive oxygen species (ROS) within the cell. This protein is essential for the proper folding of immunoglobulins and plays a significant role in ER stress-induced apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1, particularly in a CHOP-dependent manner. Additionally, ERO1L participates in the release of unfolded cholera toxin during V. cholerae infection, contributing to the retrotranslocation of the toxin.

ERO1-Like Protein Alpha; ERO1-L; ERO1-L-Alpha; Endoplasmic Oxidoreductin-1-Like Protein; Oxidoreductin-1-L-Alpha; ERO1L

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.