ARG62468

anti-DNA polymerase beta antibody [18S]

anti-DNA polymerase beta antibody [18S] for Western blot,Immunohistochemistry,IHC-Formalin-fixed paraffin-embedded sections,Immunoprecipitation and Mouse,Rat,Hamster,Bovine,Human,Xenopus laevis

Gene Regulation antibody

Overview

Product Description Mouse Monoclonal antibody [18S] recognizes DNA polymerase beta
Tested Reactivity Hu, Ms, Rat, Bov, Hm, Xenopus laevis
Tested Application IHC, IHC-P, IP, WB
Host Mouse
Clonality Monoclonal
Clone 18S
Isotype IgG1
Target Name DNA polymerase beta
Antigen Species Rat
Immunogen Rat DNA polymerase beta full length protein (Rat)
Conjugation Un-conjugated
Alternate Names EC 4.2.99.-; EC 2.7.7.7; DNA polymerase beta

Application Instructions

Application Note WB: 1-2 ug/ml
IHC: 1/10-1/500
IP: 2 ug/ml
* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.

Properties

Form Liquid
Buffer 10mM PBS (pH 7.4) and 0.2% BSA
Stabilizer 0.2% BSA
Concentration 0.2 mg/ml
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 18970 Mouse POLB

GeneID: 29240 Rat POLB

GeneID: 397973 Xenopus laevis POLB

Gene Symbol Polb
Gene Full Name polymerase (DNA directed), beta
Background The protein encoded by this gene is a DNA polymerase involved in base excision and repair, also called gap-filling DNA synthesis. The encoded protein, acting as a monomer, is normally found in the cytoplasm, but it translocates to the nucleus upon DNA damage. Several transcript variants of this gene exist, but the full-length nature of only one has been described to date. [provided by RefSeq, Sep 2011]
Function Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. [UniProt]
Cellular Localization Nucleus
Research Area Gene Regulation antibody
Calculated MW 38 kDa
PTM Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.
Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation.

Clone References

Base excision repair defects invoke hypersensitivity to PARP inhibition.

IP / Mouse

Horton JK et al.
Mol Cancer Res.,  (2014)

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Differential regulation of S-region hypermutation and class-switch recombination by noncanonical functions of uracil DNA glycosylase.

Yousif AS et al.
Proc Natl Acad Sci U S A.,  (2014)

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hr_line

An inverse switch in DNA base excision and strand break repair contributes to melphalan resistance in multiple myeloma cells.

WB / Human

Sousa MM et al.
PLoS One.,  (2013)

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Oxidative stress alters base excision repair pathway and increases apoptotic response in apurinic/apyrimidinic endonuclease 1/redox factor-1 haploinsufficient mice.

WB / Mouse

Unnikrishnan A et al.
Free Radic Biol Med.,  (2009)

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DNA polymerase beta is able to repair breaks in switch regions and plays an inhibitory role during immunoglobulin class switch recombination.

WB, ChIP / Mouse

Wu X et al.
J Exp Med.,  (2007)

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A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment.

ChIP / Human

Luo H et al.
Mol Cell Biol.,  (2004)

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Oxidative DNA damage and repair in experimental atherosclerosis are reversed by dietary lipid lowering.

WB / Rabbit

Martinet W et al.
Circ Res.,  (2001)

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