Introduction
REXO1, also known as RNA exonuclease 1 homolog, is a protein involved in RNA metabolism. It interacts with the Elongin complex, which plays a crucial role in regulating transcription elongation by RNA polymerase II. This complex enhances transcription by reducing pausing of the polymerase during its movement along the DNA template. REXO1, consisting of 1221 amino acids, is widely expressed in various tissues. Its presence is particularly notable in embryonic and adult stem cells, suggesting its potential importance in stem cell biology.
Description
This product consists of a recombinant human REXO1 protein produced in E. coli. It is a single polypeptide chain that lacks glycosylation and comprises 198 amino acids (spanning positions 1060 to 1221). The protein has a molecular weight of 22.3 kDa. For purification and detection purposes, a 36-amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for clarity.
Formulation
The REXO1 protein is supplied in a solution at a concentration of 0.25 mg/ml. The solution is buffered with 20 mM Tris-HCl at pH 8.0 and contains 0.15 M NaCl, 10% glycerol, and 1 mM DTT.
Stability
For short-term storage (up to 4 weeks), the product can be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the REXO1 protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSIYAL DCEMSYTTYG LELTRVTVVD TDVHVVYDTF VKPDNEIVDY NTRFSGVTEA DLADTSVTLR DVQAVLLSMF SADTILIGHS LESDLLALKV IHSTVVDTSV LFPHRLGLPY KRSLRNLMAD YLRQIIQDNV DGHSSSEDAG ACMHLVIWKV REDAKTKR.