Recombinant Human ERO1L His Protein

SDS-Page: ERO1L Recombinant Protein [NBP2-51682] - 15% SDS Page (3 ug)

• Reactivity: Hu
• Applications: PAGE
• Concentration: 1 mg/ml

Recombinant Human ERO1L His Protein Summary

• Description: A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 24-468 of Human ERO1L
  
  

  Source: E.coli

  Amino Acid Sequence: 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

• Source: E. coli
• Protein/Peptide Type: Recombinant Protein
• Gene: ERO1A
• Purity: >90%, by SDS-PAGE

Applications/Dilutions

• Dilutions:
  • SDS-Page
• Theoretical MW: 54.4 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: 20 mM Tris-HCl buffer (pH 8.0), 10% glycerol
• Preservative: No Preservative
• Concentration: 1 mg/ml
• Purity: >90%, by SDS-PAGE

Alternate Names for Recombinant Human ERO1L His Protein

• EC 1.8.4
• EC 1.8.4.-
• Endoplasmic oxidoreductin-1-like protein
• ERO1 (S. cerevisiae)-like
• ERO1A
• ERO1-alpha
• ERO1L alpha
• ERO1-l alpha
• ERO1L
• ERO1-L
• ERO1-L-alpha
• ERO1-like (S. cerevisiae)
• ERO1-like alpha
• ERO1-like protein alpha
• ERO1-like
• oxidoreductin-1-L-alpha

Background

Perhaps the most distinctive feature of protein folding in the ER is the abundance of disulfide bonds that must form during maturation of proteins traveling along the secretory pathway. Formation of disulfide bonds is a redox reaction. Thus, to match the flux of disulfide bonds that exit from the ER by virtue of protein secretion, a flux of oxidizing equivalents into the ER is required. In eukaryotic cells, the essential protein relay supporting this flux, and hence disulfide bond formation, involves endoplasmic reticulum oxidoreductin 1 (Ero1) and protein disulfide isomerase (PDI). The temporal pattern of hypoxic ERO1-L alpha induction is very similar to that of genes triggered by the hypoxia inducible transcription factor (HIF-1) and is characteristically mimicked by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor translocator (ARNT, HIF-1 alpha). We speculate from these findings that the expression of ERO1-L alpha is probably regulated via the HIF-pathway and thus belongs to the family of classic oxygen regulated genes.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Bioinformatics

• Gene Symbol: ERO1A