This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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-20 °C
Genschel, Modrich: "Functions of MutLalpha, replication protein A (RPA), and HMGB1 in 5'-directed mismatch repair." in: The Journal of biological chemistry, Vol. 284, Issue 32, pp. 21536-44, (2009) (PubMed).
Sharma, Sommers, Driscoll, Uzdilla, Wilson, Brosh: "The exonucleolytic and endonucleolytic cleavage activities of human exonuclease 1 are stimulated by an interaction with the carboxyl-terminal region of the Werner syndrome protein." in: The Journal of biological chemistry, Vol. 278, Issue 26, pp. 23487-96, (2003) (PubMed).
EXO1 (exonuclease 1) is a 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. EXO1 functions in DNA mismatch repair (MMR) to excise mismatchcontaining DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5' overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5' end of a downstream Okazaki fragment. EXO1 is required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. It is essential for male and female meiosis. EXO1 interacts with the MLH1-PMS2 heterodimer via MLH1. It interacts with MSH3 and with the MSH2-MSH6 heterodimer via MSH2, and this interaction may increase the processivity of the 5'->3' exonuclease activity. EXO1 interacts with PCNA, and this interaction may both stimulate the cryptic 3'->5' exonuclease activity and suppress the 5'->3' exonuclease activity. EXO1 interacts with WRN, and this interaction stimulates both the 5'->3' exonuclease activity and cleavage of 5' overhanging flap structures. It also interacts with RECQL/RECQ1, and this interaction stimulates cleavage of 5' overhanging flap structures.