Recombinant Human POLG protein is a Human Full Length protein, in the 2 to 1239 aa range, expressed in Baculovirus infected Sf9, with >=81% purity and suitable for SDS-PAGE.
M H H H H H H D Y K D D D D K S R L L W R K V A G A T V G P G P V P A P G R W V S S S V P A S D P S D G Q R R R Q Q Q Q Q Q Q Q Q Q Q Q Q P Q Q P Q V L S S E G G Q L R H N P L D I Q M L S R G L H E Q I F G Q G G E M P G E A A V R R S V E H L Q K H G L W G Q P A V P L P D V E L R L P P L Y G D N L D Q H F R L L A Q K Q S L P Y L E A A N L L L Q A Q L P P K P P A W A W A E G W T R Y G P E G E A V P V A I P E E R A L V F D V E V C L A E G T C P T L A V A I S P S A W Y S W C S Q R L V E E R Y S W T S Q L S P A D L I P L E V P T G A S S P T Q R D W Q E Q L V V G H N V S F D R A H I R E Q Y L I Q G S R M R F L D T M S M H M A I S G L S S F Q R S L W I A A K Q G K H K V Q P P T K Q G Q K S Q R K A R R G P A I S S W D W L D I S S V N S L A E V H R L Y V G G P P L E K E P R E L F V K G T M K D I R E N F Q D L M Q Y C A Q D V W A T H E V F Q Q Q L P L F L E R C P H P V T L A G M L E M G V S Y L P V N Q N W E R Y L A E A Q G T Y E E L Q R E M K K S L M D L A N D A C Q L L S G E R Y K E D P W L W D L E W D L Q E F K Q K K A K K V K K E P A T A S K L P I E G A G A P G D P M D Q E D L G P C S E E E E F Q Q D V M A R A C L Q K L K G T T E L L P K R P Q H L P G H P G W Y R K L C P R L D D P A W T P G P S L L S L Q M R V T P K L M A L T W D G F P L H Y S E R H G W G Y L V P G R R D N L A K L P T G T T L E S A G V V C P Y R A I E S L Y R K H C L E Q G K Q Q L M P Q E A G L A E E F L L T D N S A I W Q T V E E L D Y L E V E A E A K M E N L R A A V P G Q P L A L T A R G G P K D T Q P S Y H H G N G P Y N D V D I P G C W F F K L P H K D G N S C N V G S P F A K D F L P K M E D G T L Q A G P G G A S G P R A L E I N K M I S F W R N A H K R I S S Q M V V W L P R S A L P R A V I R H P D Y D E E G L Y G A I L P Q V V T A G T I T R R A V E P T W L T A S N A R P D R V G S E L K A M V Q A P P G Y T L V G A D V D S Q E L W I A A V L G D A H F A G M H G C T A F G W M T L Q G R K S R G T D L H S K T A T T V G I S R E H A K I F N Y G R I Y G A G Q P F A E R L L M Q F N H R L T Q Q E A A E K A Q Q M Y A A T K G L R W Y R L S D E G E W L V R E L N L P V D R T E G G W I S L Q D L R K V Q R E T A R K S Q W K K W E V V A E R A W K G G T E S E M F N K L E S I A T S D I P R T P V L G C C I S R A L E P S A V Q E E F M T S R V N W V V Q S S A V D Y L H L M L V A M K W L F E E F A I D G R F C I S I H D E V R Y L V R E E D R Y R A A L A L Q I T N L L T R C M F A Y K L G L N D L P Q S V A F F S A V D I D R C L R K E V T M D C K T P S N P T G M E R R Y G I P Q G E A L D I Y Q I I E L T K G S L E K R S Q P G P
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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 (PubMed:11477093, PubMed:11897778, PubMed:15917273, PubMed:19837034, PubMed:9558343). 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 (PubMed:11477093, PubMed:11897778, PubMed:15167897, PubMed:15917273, PubMed:19837034, PubMed:26095671, PubMed:9558343). 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 (PubMed:10827171, PubMed:11477094, PubMed:11504725, PubMed:37202477). 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 (PubMed:9770471).
MDP1, POLG1, POLGA, POLG, DNA polymerase subunit gamma-1, 3'-5' exodeoxyribonuclease, 5'-deoxyribose-phosphate lyase, Mitochondrial DNA polymerase catalytic subunit, PolG-alpha
Recombinant Human POLG protein is a Human Full Length protein, in the 2 to 1239 aa range, expressed in Baculovirus infected Sf9, with >=81% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.04% Sorbitan monolaurate, ethoxylated, 0.02% Potassium chloride
Affinity purified.
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 (PubMed:11477093, PubMed:11897778, PubMed:15917273, PubMed:19837034, PubMed:9558343). 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 (PubMed:11477093, PubMed:11897778, PubMed:15167897, PubMed:15917273, PubMed:19837034, PubMed:26095671, PubMed:9558343). 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 (PubMed:10827171, PubMed:11477094, PubMed:11504725, PubMed:37202477). 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 (PubMed:9770471).
Belongs to the DNA polymerase type-A family.
This product was previously labelled as DNA Polymerase gamma
POLG also known as DNA polymerase gamma is an enzyme essential for mitochondrial DNA replication and repair. It is composed of a catalytic subunit with approximately 140 kDa mass. This protein is mainly expressed in tissues with high energy demands such as liver heart and skeletal muscles. POLG functions by synthesizing the leading and lagging strands during mitochondrial DNA replication ensuring mitochondrial DNA integrity.
DNA polymerase gamma plays an important role in maintaining mitochondrial genomes. This protein operates within a complex called the POLG complex which is vital for mitochondrial DNA replication machinery. The catalytic subunit works alongside two accessory subunits that enhance its processivity and accuracy during DNA synthesis. Mutations in POLG can impair mitochondrial DNA replication leading to mitochondrial dysfunction.
POLG is integral in the mitochondrial DNA replication and repair pathways. It is closely linked with the pathways ensuring mitochondrial gene expression and energy production. POLG acts in concert with mitochondrial DNA helicase TWINKLE and mitochondrial single-stranded DNA binding protein (mtSSB) both contributing to the replication fork activity and stability. POLG's role ensures proper mitochondrial function and consequently cellular energy homeostasis.
POLG mutations have been associated with diverse mitochondrial disorders including Alpers-Huttenlocher syndrome and progressive external ophthalmoplegia. POLG-related disorders often result from impaired mitochondrial DNA replication leading to energy deficits in cells. In particular mutations affecting the POLG complex's performance can influence the onset of these conditions sometimes involving interactions with other proteins like TWINKLE and mtSSB which further complicate the mitochondrial dysfunction seen in such diseases.
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SDS-PAGE analysis of 1.3 μg ab196066 using 4-20 % SDS-PAGE gel and stained with Coomassie.
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