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AB111641

Recombinant Human DNA Polymerase beta protein (His tag N-Terminus)

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Recombinant Human DNA Polymerase beta protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 335 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

대체 명칭 보기

DNA polymerase beta, 5'-deoxyribose-phosphate lyase, AP lyase, 5'-dRP lyase, POLB

1 이미지
SDS-PAGE - Recombinant Human DNA Polymerase beta protein (His tag N-Terminus) (AB111641)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human DNA Polymerase beta protein (His tag N-Terminus) (AB111641)

15% SDS-PAGE analysis of ab111641 (3 μg)

주요 정보

Purity

>90% SDS-PAGE

ab111641 is purified using conventional chromatography.

발현 시스템

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Animal free

No

Carrier free

No

Species

Human

보관 버퍼

pH: 8 Constituents: 69% Tris HCl, 30% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity 정보

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

서열 정보

[{"linker":null,"sequence":"MGSSHHHHHHSSGLVPRGSHMSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE","proteinLength":"Full Length","predictedMolecularWeight":"40.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":335,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P06746","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

특성 및 보관 정보

제형
Liquid
배송 시 보관 조건
Blue Ice
적절한 단기 보관 기간
1-2 weeks
적절한 단기 보관 조건
+4°C
적절한 장기 보관 조건
-20°C
분주 정보
Upon delivery aliquot
보관 정보
Avoid freeze / thaw cycle
False

추가 정보

This supplementary information is collated from multiple sources and compiled automatically.

DNA polymerase beta often abbreviated as pol β serves as a repair enzyme that plays a role in the base excision repair (BER) pathway. This protein's mechanical function involves filling small gaps in the DNA created during repair processes by adding nucleotides. Its molecular weight is approximately 39 kDa. DNA polymerase beta is expressed extensively in the brain liver and testis indicating its importance in DNA repair in various cells. Other names for this protein include DNA pol beta and pol β. It synthesizes DNA using deoxyribonucleotide triphosphates as substrates and requires magnesium ions for activity.
Biological function summary

DNA polymerase beta helps to maintain genome integrity by repairing DNA lesions caused by oxidation alkylation or deamination. This protein often collaborates with other components of the DNA repair pathways but it does not directly form a larger protein complex focusing instead on its important function in BER. When DNA damage like single-strand breaks occur pol β carries out important gap-filling synthesis steps preparing the strand for subsequent ligation.

Pathways

DNA polymerase beta functions critically in base excision repair and acts alongside other important proteins like XRCC1. The BER pathway operates to correct DNA damage from endogenous sources preventing harmful mutations. This pathway is essential for maintaining cellular stability and protecting cells from apoptosis or malignant transformation that might occur if DNA damage propagates.

Mutations or dysfunctional activity within DNA polymerase beta have links to cancer and neurodegenerative diseases. For example errors in pol β's repair functions can lead to the persistence of DNA damage which can contribute to tumorigenesis. Furthermore its relationship with beta-actin has implications in cellular structural integrity and cancer metastasis. Dysfunctions within the BER pathway indicate potential contributions to neurodegenerative disorders where an accumulation of DNA damage is a common feature.

일반 정보

기능

Repair polymerase that plays a key role in base-excision repair (PubMed : 10556592, PubMed : 9207062, PubMed : 9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed : 10556592, PubMed : 17526740, PubMed : 9556598, PubMed : 9572863, PubMed : 9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed : 9614142).

서열 유사성

Belongs to the DNA polymerase type-X family.

Post-translational modifications

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.

Subcellular localisation

Nucleus

제품 프로토콜

타겟 정보

Repair polymerase that plays a key role in base-excision repair (PubMed : 10556592, PubMed : 9207062, PubMed : 9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed : 10556592, PubMed : 17526740, PubMed : 9556598, PubMed : 9572863, PubMed : 9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed : 9614142).
See full target information POLB

Product promise

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