POLK Antibody, FITC conjugated

說明書

中文名稱：

POLK兔多克隆抗體, FITC偶聯(lián)
貨號：

CSB-PA887009LC01HU
規(guī)格：

￥880
其他：

產(chǎn)品詳情
產(chǎn)品評價
相關(guān)產(chǎn)品
靶點詳情

產(chǎn)品詳情

產(chǎn)品名稱：

Rabbit anti-Homo sapiens (Human) POLK Polyclonal antibody
Uniprot No.：

Q9UBT6
基因名：

POLK
別名：

DinB homolog 1 (E. coli) antibody; DINB protein antibody; DINB1 antibody; DINP antibody; DNA damage inducible protein b antibody; DNA polymerase kappa antibody; Polk antibody; POLK_HUMAN antibody; POLQ antibody; Polymerase (DNA directed) kappa antibody; polymerase, DNA, kappa antibody
宿主：

Rabbit
反應(yīng)種屬：

Human
免疫原：

Recombinant Human DNA polymerase kappa protein (227-337AA)
免疫原種屬：

Homo sapiens (Human)
標(biāo)記方式：

FITC
克隆類型：

Polyclonal
抗體亞型：

IgG
純化方式：

>95%, Protein G purified
濃度：

It differs from different batches. Please contact us to confirm it.
保存緩沖液：

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
產(chǎn)品提供形式：

Liquid
儲存條件：

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期：

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
用途：

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產(chǎn)品評價

靶點詳情

功能：

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. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.
基因功能參考文獻：
1. This study found that human DNA Polymerase kappa is more tolerant to changes in the active site loop than E. coli DinB. [DinB] PMID: 28823149
2. Two X-ray crystal structures of POLK provide mechanistic insights into the error-free lucidin-N(2)-dG DNA adduct bypass catalyzed by POLK. PMID: 28972744
3. POLH & POLK are both able to exchange with PolD1 stalled at repetitive CFS (common fragile sites) sequences. POLD1 synthesis was inhibited by replication stress caused by aphidicolin, preventing any replication past CFS. Importantly, POLH & POLK were still proficient in rescuing this stalled POLD1 synthesis. POLD1 stalling at CFSs allows for free exchange with specialized polymerase that is not driven by PCNA. PMID: 28605669
4. The structure of polK captured at the lesion-extension stage is reported: the enzyme is extending the primer strand after the base pair containing the BP-dG adduct in the template strand at the -1 position. PolK accommodates the BP adduct in the nascent DNA's minor groove and keeps the adducted DNA helix in a B-form. PMID: 27894903
5. A report on the structure of human polkappa in complex with a major benzo[a]pyrene adduct reveal a unique mechanism for accurate replication by translesion synthesis past the major bulky adduct. PMID: 27034468
6. These studies revealed that POLK is a crucial host factor required for covalently closed circular DNA formation during a de novo HBV infection PMID: 27783675
7. DNA polymerases eta and kappa are capable of bypassing of a bulky guanine lesion during DNA replication. PMID: 27612622
8. POLK protein polymorphisms may influence the risk of developing breast cancer among Chinese women. PMID: 26765445
9. Somatic Mutations in Catalytic Core of POLK Reported in Prostate Cancer Alter Translesion DNA Synthesis PMID: 26046662
10. POLK not only protects cells from genotoxic DNA lesions via DNA polymerase activities, but also contributes to genome integrity by acting as a non-catalytic protein against oxidative damage caused by hydrogen peroxide and menadione. PMID: 26031400
11. The steric gate is crucial for rNTP discrimination because of its role in specifically promoting a dNTP-induced conformational change and that rNTP discrimination occurs in a relatively closed state of the polymerases. PMID: 25684709
12. The structural dynamics of DinB1 changes upon substrate binding, noncognate DNA damage prevents the formation of the active conformation of DINB1. PMID: 25899385
13. polymorphism of POLK, an important gene in TLS, participates in platinum-chemotherapy tolerance and side-effect PMID: 24948471
14. The study shows that the Werner syndrome protein stimulates the 8-oxo-dG bypass activity of hpol kappa in vitro by enhancing the correct base insertion opposite the lesion, as well as extension from dC:8-oxo-dG base pairs. PMID: 25294835
15. Mutations in PIP1 domain inhibits the stimulation of DNA synthesis by Polkappa in the presence of proliferating cell nuclear antigen, replication factor C, and replication protein A; and mutations in PIP2 have no effect on PCNA-dependent DNA synthesis. PMID: 24848457
16. The truncation R219X was devoid of polymerase activity, and the E419G and Y432S variants showed much lower polymerase activity than wild-type POLK. PMID: 24725253
17. A slow conformational change after the nucleotidyl transfer is the rate-limiting step for hpol kappa catalysis. PMID: 25065501
18. role of the unique Polkappa gap and N-clasp structural features in the fidelity of minor groove lesion processing with extensive molecular modeling and molecular dynamics simulations to pinpoint their functioning in lesion bypass PMID: 25148552
19. Phenylalanine 171 is used by PolK as a molecular brake for translesional synthesis across benzo[a]pyrene DNA adducts. PMID: 24461735
20. The molecular mechanism of 3-nitrobenzanthrone genotoxicity in HEK293 cells is reported. PMID: 25080294
21. DNA polymerase kappa rs5744724 polymorphism is associated with lung cancer. PMID: 24012694
22. Pol eta and Pol kappa are involved in redundant pathways for homologous recombination. PMID: 23731732
23. DNA polymerase kappa-dependent DNA synthesis at stalled replication forks is important for CHK1 activation. PMID: 23799366
24. The results show that hPolkappa uses a classical Streisinger template-slippage mechanism to generate -1 deletions in repetitive sequences. PMID: 23558743
25. Data indicate that small molecule library screens targeting DNA polymerase kappa would initiate the development of new adjunct cancer therapeutics. PMID: 23056190
26. Molecular dynamics simulations show that the near error-free incorporation of dCTP opposite the major benzo[a]pyrene-derived dG lesion is compatible with the Water Mediated and Substrate Assisted (WMSA) mechanism, allowing for an essentially undisturbed pentacovalent phosphorane transition state, and explaining the bypass of this lesion with little mutation by Pol kappa. PMID: 22772988
27. Data suggest that DNA polymerase kappa (pol kappa) partially protects cells from the mismatch repair (MMR)-dependent cytotoxicity. PMID: 22487424
28. The expression of Pol kappa (and Pol iota) is deregulated in gliomas, and upregulation of Pol kappa is associated with poorer prognosis in glioma patients. PMID: 20164241
29. transcriptional activities of the POLK promoter regions -336/+437 and +20/+437 were significantly reduced by BPDE treatment, indicating that transcription factors in these regions may regulate the transcription of human POLK gene in response to BPDE. PMID: 22227292
30. show that the loss of USP1 leads to a dramatic reduction of replication fork speed in a Polkappa-dependent manner PMID: 22157819
31. the substitution of alanine for phenylalanine 171 (F171), an amino acid conserved between Pol kappa and its bacterial counterpart Escherichia coli DinB, enhanced the efficiencies of dCMP incorporation opposite (-)- and (+)-trans-anti-BPDE-N(2)-dG 18-fold PMID: 21078407
32. Data show that showed that pol kappaDeltaC was more efficient than pol eta by incorporating dCMP opposite both 6alpha- and 6beta-isomeric dG-N(2)-6-E(2) adducts. PMID: 18512958
33. results suggested that amino acids at distinct positions in the active sites of Poleta and Polkappa might enhance 8-oxo-dGTP to favor the syn conformation, and thus direct its misincorporation into DNA. PMID: 19939936
34. a role of Pol(kappa) in the extension of mismatched base pairs during normal DNA replication, and in addition, they implicate Pol(kappa) in the mutagenic bypass of T-T dimers PMID: 11842189
35. Translesion synthesis by human DNA polymerase kappa on a DNA template containing a single stereoisomer of dG-(+)- or dG-(-)-anti-N(2)-BPDE. PMID: 11994005
36. In DNA damage, this protein bypasses and extends beyond thymine glycols during DNA synthesis in vitro, preferentially incorporating correct nucleotides PMID: 12145297
37. Polkappa may function as part of the replication machinery itself and could be recruited when replicative complexes are stalled; may affect the accuracy of DNA replication PMID: 12414988
38. Opposite an 8-oxoguanine (8-oxoG) lesion, Polkappa efficiently inserts an A & then proficiently extends from it. Also, Polkappa can perform the extension step after the incorporation of nucleotides opposite these lesion sites by Poldelta. PMID: 12444249
39. Data suggest that the properties of DNA polymerases eta and kappa are consistent with the mutagenic events attributed to estrogen-derived DNA adducts. PMID: 15147214
40. POLK interacts with a C-terminal region of REV1. PMID: 15189446
41. POLK does not colocalize in replication foci with PCNA. PMID: 15601657
42. the trans-lesion synthesis enzyme polkappa is specifically required for normal recovery from the BPDE-induced S-phase checkpoint PMID: 15817457
43. POLK causes error-prone and inefficient replication across 8-oxoguanine in ras genes. PMID: 15938713
44. DNA polymerase kappa (Pol kappa) is a specialised low-fidelity DNA polymerase. It is able to perform DNA synthesis across several damaged bases. But when it is misregulated, it will increase genetic instability. PMID: 15989980
45. both Poleta and Polkappa rely on W-C hydrogen bonding for localizing the nascent base pair in the active site for the polymerization reaction to occur PMID: 16055723
46. Association of Polkappa with PCNA is regulated by Rad18-mediated PCNA ubiquitination. PMID: 16611994
47. pol kappa is resistant to N(2)-bulk and quantitatively efficient in catalyzing dCTP incorporation opposite bulky guanine N(2)-adducts, particularly the largest (N(2)-BPG) PMID: 16751196
48. promoter of POLK is cis-controlled PMID: 17099721
49. DNA encirclement and other structural features help explain Pol kappa's ability to extend mismatches and to promote replication through various minor groove DNA lesions. PMID: 17317631
50. Human DNA polymerase kappa inserts dGMP and dCMP within the [T](11) mononucleotide repeat, producing an interrupted 12-bp allele. PMID: 18079151
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亞細胞定位：

Nucleus.
蛋白家族：

DNA polymerase type-Y family
組織特異性：

Detected at low levels in testis, spleen, prostate and ovary. Detected at very low levels in kidney, colon, brain, heart, liver, lung, placenta, pancreas and peripheral blood leukocytes.
數(shù)據(jù)庫鏈接：

HGNC: 9183

OMIM: 605650

KEGG: hsa:51426

STRING: 9606.ENSP00000241436

UniGene: Hs.135756

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