Recombinant Human REXO1 His Protein Summary
Description |
A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 1060-1221 of Human REXO1 Source: E.coli Amino Acid Sequence: MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSIYAL DCEMSYTTYG LELTRVTVVD TDVHVVYDTF VKPDNEIVDY NTRFSGVTEA DLADTSVTLR DVQAVLLSMF SADTILIGHS LESDLLALKV IHSTVVDTSV LFPHRLGLPY KRSLRNLMAD YLRQIIQDNV DGHSSSEDAG ACMHLVIWKV REDAKTKR |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein |
Gene |
REXO1 |
Purity |
>90%, by SDS-PAGE |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
22.3 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), 0.15 M NaCl, 10% glycerol, 1 mM DTT |
Preservative |
No Preservative |
Concentration |
0.25 mg/ml |
Purity |
>90%, by SDS-PAGE |
Alternate Names for Recombinant Human REXO1 His Protein
Background
REXO1 or Elongin A-binding protein 1 (EloA-BP1) is an exonuclease domain-containing protein that can bind to Elongin. The Elongin complex stimulates the rate of transcription elongation by RNA polymerase II by suppressing the transient pausing of the polymerase at many sites along the DNA template. REXO1 is composed of 1221 amino acids and its mRNA is ubiquitously expressed. EloA-BP1 is capable of binding not only the NH(2)-terminal approximately 120 amino acid region of Elongin A, but also that of SII. Although REXO1 had no detectable effect on the rate of transcription elongation in vitro, it may play some role in the regulation of elongation in vivo.
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.
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