Catalytic subunit of DNA polymerase gamma solely responsible for replication of mitochondrial DNA (mtDNA). Replicates both heavy and light strands of the circular mtDNA genome using a single-stranded DNA template, RNA primers and the four deoxyribonucleoside triphosphates as substrates . Has 5'' -> 3'' polymerase activity. Functionally interacts with TWNK and SSBP1 at the replication fork to form a highly processive replisome, where TWNK unwinds the double-stranded DNA template prior to replication and SSBP1 covers the parental heavy strand to enable continuous replication of the entire mitochondrial genome. A single nucleotide incorporation cycle includes binding of the incoming nucleotide at the insertion site, a phosphodiester bond formation reaction that extends the 3''-end of the primer DNA, and translocation of the primer terminus to the post-insertion site. After completing replication of a mtDNA strand, mediates 3'' -> 5'' exonucleolytic degradation at the nick to enable proper ligation . Highly accurate due to high nucleotide selectivity and 3'' -> 5'' exonucleolytic proofreading. Proficiently corrects base substitutions, single-base additions and deletions in non-repetitive sequences and short repeats, but displays lower proofreading activity when replicating longer homopolymeric stretches. Exerts exonuclease activity toward single-stranded DNA and double-stranded DNA containing 3''-terminal mispairs. When a misincorporation occurs, transitions from replication to a pro-nucleolytic editing mode and removes the missincorporated nucleoside in the exonuclease active site. Proceeds via an SN2 nucleolytic mechanism in which Asp-198 catalyzes phosphodiester bond hydrolysis and Glu-200 stabilizes the leaving group. As a result the primer strand becomes one nucleotide shorter and is positioned in the post-insertion site, ready to resume DNA synthesis . Exerts 5''-deoxyribose phosphate (dRP) lyase activity and mediates repair-associated mtDNA synthesis (gap filling) in base-excision repair pathway. Catalyzes the release of the 5''-terminal 2-deoxyribose-5-phosphate sugar moiety from incised apurinic/apyrimidinic (AP) sites to produce a substrate for DNA ligase. The dRP lyase reaction does not require divalent metal ions and likely proceeds via a Schiff base intermediate in a beta-elimination reaction mechanism .

P54098

5428

DNA polymerase subunit gamma-1, Mitochondrial DNA polymerase catalytic subunit, PolG-alpha, POLG, MDP1, POLG1, POLGA

Human,Mouse,Rat

WB,IHC,IF,ICC,FC

WB 1:1000
IHC 1:100-500
IF 1:10-50
ICC 1:10-50
FC 1:10-50

140 kD

Rabbit

Polyclonal

Rabbit IgG

This antibody is purified by peptide affinity purification.

PBS (pH7.4) with 0.09% (W/V) sodium azide.

Store at -20°C. Stable for 12 months from date of receipt.Do not aliquot the antibody.Avoid freeze / thaw cycle.