DNA pol ι rabbit pAb - 50 μL

Catalytic activity: Deoxynucleoside triphosphate + DNA (n) = diphosphate + DNA (n+1). Cofactor: Magnesium. Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. function: Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity. similarity: Belongs to the DNA polymerase type-Y family. similarity: Contains 1 umuC domain. subcellular location: Accumulates at replication forks after DNA damage. subunit: Binds REV1L (By similarity). Binds POLH. tissue specificity: Ubiquitous. Highly expressed in testis.