RAD1 Human
Description
RAD1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-282 a.a.) and having a molecular mass of 33.9 kDa. The RAD1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP MPGTLTALRM CYQGYGYPLM LFLEEGGVVT VCKINTQEPE ETLDFDFCST NVINKIILQS
EGLREAFSEL DMTSEVLQIT MSPDKPYFRL STFGNAGSSH LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES.
Product Science Overview
Recombinant Human RAD1 protein is typically expressed in Escherichia coli and is available in full-length form, ranging from amino acids 1 to 282 . The protein is often tagged with His tags at the N-terminus and/or C-terminus to facilitate purification and detection . The recombinant form of RAD1 is usually purified to a high degree of purity (>85%) and is suitable for various applications such as SDS-PAGE and mass spectrometry .
RAD1 is a part of the 9-1-1 complex, which also includes RAD9 and HUS1. This complex is recruited to sites of DNA damage by the RAD17-replication factor C (RFC) clamp loader complex . Once recruited, the 9-1-1 complex acts as a sliding clamp platform on DNA, facilitating the recruitment and stabilization of various proteins involved in long-patch base excision repair (LP-BER) .
The 9-1-1 complex enhances the activity of DNA polymerase beta (POLB) by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB at sites where LP-BER occurs . Additionally, it stimulates the endonuclease activity of FEN1 on substrates with double, nick, or gap flaps of distinct sequences and lengths, and the activity of DNA ligase I (LIG1) on LP-BER substrates .
The RAD1 protein, through its role in the 9-1-1 complex, is essential for the proper functioning of the DNA damage checkpoint and repair pathways. It helps maintain genomic integrity by ensuring that damaged DNA is accurately repaired before cell division proceeds. This function is critical in preventing mutations that could lead to various diseases, including cancer.
Recombinant Human RAD1 protein is widely used in research to study DNA repair mechanisms, cell cycle regulation, and the molecular basis of genomic stability. It is also utilized in various biochemical assays and structural studies to understand its interaction with other proteins and DNA.
