protein

EPO1L, 24-468aa, Human, His tag, E Coli

MBS205679

0.1 mg

310 USD

Recombinant Protein

EPO1L, 24-468aa, Human, His tag, E Coli

EPO1L

ERO1-like protein alpha; ERO1-alpha; ERO1A

ERO1-like protein alpha; ERO1-like protein alpha; ERO1-like protein alpha; endoplasmic oxidoreductin-1-like protein; oxidoreductin-1-L-alpha; ERO1-like (S. cerevisiae); Endoplasmic oxidoreductin-1-like protein; Oxidoreductin-1-L-alpha

EPO1L

ERO1L; ERO1L; ERO1A; ERO1-L; ERO1LA; ERO1-alpha; ERO1-L-alpha; ERO1-L; ERO1-L-alpha

ERO1A_HUMAN

468

MGSSHHHHHH SSGLVPRGSH MGSEEQPPET AAQRCFCQVS GYLDDCTCDV ETIDRFNNYR LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA VKPCQSDEVP DGIKSASYKY SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEADD IQSPEAEYVD LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL CVEKRAFYRL ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE IKSFPLHFDE NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW GKLQTQGLGT ALKILFSEKL IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH

> 90% by SDS - PAGE

Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 10% glycerol

1 mg/ml (determined by Bradford assay)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human. Tag: His-tag

Expression System: E Coli

Signal Transduction

ERO1-like protein alpha, also known as EPO1L, is an essential oxidoreductase that oxidizes proteins and is required for the folding of immunoglobulins. EPO1L covalently binds with PDI (protein disulfide-isomerase) and together they produce disulfide bonds between proteins in the endoplasmic reticulum. EPO1L is stimulated by hypoxia, suggesting that it is regulated through the HIF (hypoxia inducible transcrip-tion factor) pathway. EPO1L is ubiquitously expressed at low levels but expressed at high levels in upper digestive tract and esophagus. Recombinant human EPO1L protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Otsu M., et al. (2006) Antioxid. Redox Signal. 8: 274-282. Gess B., et al. (2003) J Biochem. 270: 2228-2235.

7657069

NP_055399

NM_014584.2

54.4 kDa (468aa)

Cellular Responses To Stress Pathway (645258); Detoxification Of Reactive Oxygen Species Pathway (1127552); Insulin Processing Pathway (105903); Metabolism Of Proteins Pathway (106230); Peptide Hormone Metabolism Pathway (771603); Protein Processing In Endoplasmic Reticulum Pathway (167325); Protein Processing In Endoplasmic Reticulum Pathway (167190); Vibrio Cholerae Infection Pathway (83101); Vibrio Cholerae Infection Pathway (513)

ERO1L: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys- 99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. Belongs to the EROs family. Protein type: Secreted, signal peptide; Oxidoreductase; EC 1.8.4.-; Secreted. Chromosomal Location of Human Ortholog: 14q22.1. Cellular Component: endoplasmic reticulum membrane; intracellular membrane-bound organelle; membrane; endoplasmic reticulum lumen; endoplasmic reticulum. Molecular Function: protein binding; protein disulfide oxidoreductase activity; protein disulfide isomerase activity; oxidoreductase activity; oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor. Biological Process: protein maturation via protein folding; extracellular matrix organization and biogenesis; chaperone cofactor-dependent protein folding; protein folding; unfolded protein response; protein modification process; response to temperature stimulus; response to reactive oxygen species; 4-hydroxyproline metabolic process; cellular protein metabolic process; cell redox homeostasis; release of sequestered calcium ion into cytosol; brown fat cell differentiation

0.1 mg

310 USD

0.5 mg

720