Recombinant Human DNA damage-binding protein 1 (DDB1), partial
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中文名稱：Recombinant Human DNA damage-binding protein 1(DDB1) ,partial
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貨號：CSB-YP618079HU
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說明書：
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規格：
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來源：Yeast
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其他：
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中文名稱：Recombinant Human DNA damage-binding protein 1(DDB1) ,partial
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貨號：CSB-EP618079HU
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說明書：
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規格：
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來源：E.coli
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其他：
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中文名稱：Recombinant Human DNA damage-binding protein 1(DDB1) ,partial
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貨號：CSB-EP618079HU-B
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說明書：
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規格：
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來源：E.coli
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共軛：Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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其他：
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中文名稱：Recombinant Human DNA damage-binding protein 1(DDB1) ,partial
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貨號：CSB-BP618079HU
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說明書：
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規格：
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來源：Baculovirus
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其他：
產品詳情
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純度：>85% (SDS-PAGE)
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基因名：
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Uniprot No.：
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別名：Damage specific DNA binding protein 1; Damage-specific DNA-binding protein 1; DDB 1; DDB p127 subunit; Ddb1; DDB1_HUMAN; DDBa; DNA damage binding protein 1; DNA damage-binding protein 1; DNA damage-binding protein a; HBV X-associated protein 1; UV damaged DNA binding factor; UV damaged DNA binding protein 1; UV DDB 1; UV DDB1 ; UV-damaged DNA-binding factor; UV-damaged DNA-binding protein 1; UV-DDB 1; X associated protein 1; XAP 1; XAP-1; XAP1; Xeroderma pigmentosum group E complementing protein; Xeroderma pigmentosum group E-complementing protein; XPCe; XPE; XPE BF; XPE binding factor; XPE-BF; XPE-binding factor
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種屬：Homo sapiens (Human)
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蛋白長度：Partial
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蛋白標簽：Tag?type?will?be?determined?during?the?manufacturing?process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially. -
產品提供形式：Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand. -
復溶：We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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儲存條件：Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保質期：The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. -
貨期：Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
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注意事項：Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Datasheet ：Please contact us to get it.
產品評價
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靶點詳情
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功能：Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver.
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基因功能參考文獻：
- These results suggest that different DDB1-CUL4 associated factors play distinct roles in human lung adenocarcinoma development. PMID: 28336923
- The DDB1 is acetylated and acetylation promotes DDB1 binding to CUL4. PMID: 28886238
- Results revealed a function independent of its transcriptional activity, as TTF-1 was found to interact with DDB1 and block its binding to CHK1, which in turn attenuated ubiquitylation and subsequent degradation of CHK1. PMID: 28192407
- SIRT7 inhibits TR4 degradation by deacetylation of DDB1. PMID: 28623141
- the c-Abl non-receptor kinase phosphorylates DDB1 at residue Tyr-316 to recruit a small regulatory protein, DDA1, leading to increased substrate ubiquitination PMID: 28087699
- knockdown of DCAF7 reduced the degradation of DNA ligase I in response to inhibition of proliferation and replacement of ubiquitylated lysine residues reduced the in vitro ubiquitylation of DNA ligase I by Cul4-DDB1 and DCAF7. In contrast, a different E3 ubiquitin ligase regulates FEN-1 turnover. PMID: 27573245
- This study presents the crystal structure of the DDB1-DCAF1-HIV-1-Vpr-uracil-DNA glycosylase (cyclin U) complex. PMID: 27571178
- Our data are consistent with the idea that the CUL4A/B-DDB1-CRBN complex catalyses the polyubiquitination and thus controls the degradation of CLC-1 channels. PMID: 26021757
- These results revealed a novel role of DDB in H3K56Ac deacetylation during early step of NER and the existence of active functional cross-talk between DDB-mediated damage recognition and H3K56Ac deacetylation. PMID: 26255936
- The identification of Vpr mutants which associate with DCAF1 but only poorly with DDB1 suggests that DCAF1 is necessary but is not sufficient for the Vpr association with DDB1-containing E3 ligase complex. PMID: 24912982
- Data support a model wherein DDB1 and DDB2 cooperate to repress Bcl-2 transcription. DDB2 recognizes and binds to the Bcl-2 P1 promoter, and HDAC1 is recruited through the DDB1 subunit associated with DDB2 to deacetylate histone H3K9. PMID: 24249678
- The study presents the crystal structure of human CRBN bound to DDB1 and the drug lenalidomide. PMID: 25108355
- CUL4A-DDB1-Rbx1 E3 ligase controls the quality of the PTS2 receptor Pex7p. PMID: 24989250
- structures of the DDB1-CRBN complex bound to thalidomide, lenalidomide and pomalidomide PMID: 25043012
- In the three intrinsically IMiD-resistant cell lines that clearly express detectable levels of cereblon, the absence of CRBN and DDB1 mutations suggest that potential cereblon-independent mechanisms of resistance exist PMID: 24166296
- UV-DDB examines sites on DNA in discrete steps before forming long-lived, nonmotile UV-DDB dimers (DDB1-DDB2)2 at sites of damage. PMID: 24760829
- p73 interacts with the CDL4A complex by binding directly to DDB1. The CDL4A complex is able to monoubiquitylate p73, negatively affecting its transcriptional function. PMID: 23085759
- As a molecular adaptor, Vpr enhanced the interaction between TERT and the VPRBP substrate receptor of the DYRK2-associated EDD-DDB1-VPRBP E3 ligase complex, resulting in increased ubiquitination of TERT. PMID: 23612978
- Data indicate that Dyrk2 phosphorylates TERT protein, which is then associated with the EDD-DDB1-VprBP E3 ligase complex for subsequent ubiquitin-mediated TERT protein degradation. PMID: 23362280
- Our findings suggest that DDB1 is a cellular substrate of NS3/4A required for Hepatitis c viurs replication. PMID: 23137809
- The EZH2-DCAF1/DDB1/CUL4 represents a previously unrecognized methylation-dependent ubiquitination machinery specifically recognizing "methyl degron"; nonhistone protein stability can be dynamically regulated in a methylation-dependent manner. PMID: 23063525
- potential GRK5 interacting proteins and the association of GRK5 with DDB1 in cell and the regulation of GRK5 level by DDB1-CUL4 ubiquitin ligase complex-dependent proteolysis pathway PMID: 22952844
- Findings indicate structural and conformational insights of the DDB1-CUL4A(DDB2) E3 ligase, with significant implications for the regulation and overall organization of the proteins responsible for initiation of nucleotide-excision repair (NER) pathway. PMID: 22822215
- The data suggested that HomolD-containing promoters require the RNA polymerase II machinery and the proteins DDB1 and RECQL for accurate transcription. PMID: 22705827
- Hepatitis B virus regulatory HBx protein binding to DDB1 is required but is not sufficient for maximal HBV replication. PMID: 22342275
- crystals of CSA-DDB1 had unit-cell parameters a = b = 142.03, c = 250.19 A and diffracted to 2.9 A resolution on beamline ID14-1 PMID: 22232169
- Studies indicate the modular architecture of DDB1-CUL4 in complex with DDB2, CSA and CDT2 in DNA repair of UV-induced DNA lesions. PMID: 21550341
- damage-specific DNA binding protein 1 is essential to regulation of p27(kip1) turnover after a mild DNA damage PMID: 21237244
- the CUL4A.DDB1 E3 complex is important for regulation of RASSF1A during mitosis, and it may contribute to inactivation of RASSF1A and promoting cell cycle progression PMID: 21205828
- This review focuses on Vpr and its HIV2/SIV counterparts, Vpx and Vpr, which all engage the DDB1.Cullin4 ubiquitin ligase complex through the DCAF1 adaptor protein. PMID: 20347598
- DDB1 modulates the function of APC/C(Cdh1) in a manner independent of the Cul4-DDB1 complex PMID: 20395298
- The data suggest that DDB1 could potentially be developed into biomarkers of resistance to acyl sulfonamide-based cancer drugs. This will require clinical validation in a series of patients treated with R3200. PMID: 19723642
- Studies indicate that CUL4 uses a large beta-propeller protein, DDB1, as a linker to interact with a subset of WD40 proteins. PMID: 19818632
- Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation PMID: 12034848
- findings substantiate the physical and functional connection between the hepatitis B virus X protein and the DDB1-DDB2 heterodimer, leading to the regulation of the pool of the viral protein PMID: 12050362
- These findings indicate that hepatitis B virus X protein acts through a pathway that involves a DDB2-independent nuclear function of DDB1 and that this activity will depend on the relative concentration of DDB1 and DDB2 in cells. PMID: 12151405
- essential for the targeted degradation of STAT1 by the V protein of the paramyxovirus simian virus 5. DDB1 may form a multiprotein complex with STAT1, STAT2, and V for this degradation. PMID: 12388698
- SV5-V and HBx have evolved to bind DDB1 to achieve distinct functions in their life cycle, both by a mechanism that does not involve DDB2. PMID: 12743284
- DET1 promotes ubiquitination and degradation of c-Jun by assembling a multisubunit ubiquitin ligase containing DNA Damage Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1 (ROC1), and constitutively photomorphogenic-1 PMID: 14739464
- Damaged DNA binding protein 1 is a component of the centromere complex in interphase cells. PMID: 15009096
- results show that HBx in association with DDB1 acts in the nucleus and stimulates hepatitis B virus replication mainly by enhancing viral mRNA levels PMID: 15767425
- DDB1-DDB2 protein complex recognizes DNA mismatches and lesions PMID: 16223728
- PCNA is involved in mediating Cdt1 degradation by the Cul4-Ddb1 ligase in response to DNA damage. PMID: 16407242
- Cdt1 degradation requires predominant use of the PCNA/Cul4/Ddb1 ubiquitin ligase pathway after DNA damage PMID: 16407252
- Monoubiquitinated histone H2A in native chromatin coimmunoprecipitates with the endogenous DDB1-CUL4A(DDB2) complex in response to UV irradiation. PMID: 16473935
- The F-box protein Skp2, in addition to utilizing Cul1-Skp1, utilizes Cul4A-DDB1 to induce proteolysis of p27Kip1. PMID: 16537899
- This study uncovers CUL4-DDB-ROC1 as a histone ubiquitin ligase and demonstrate that histone H3 and H4 ubiquitylation participates in the cellular response to DNA damage. PMID: 16678110
- PCNA, L2DTL and the DDB1-CUL4A complex play critical and differential roles in regulating the protein stability of p53 and MDM2/HDM2 in unstressed and stressed cells. PMID: 16861890
- L2DTL and PCNA interact with CUL4/DDB1 complexes and are involved in CDT1 degradation after DNA damage. PMID: 16861906
- Results suggest that DDB1 prevents DNA lesions from accumulating in replicating human cells, in part by regulating Cdt1 degradation. PMID: 16940174
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亞細胞定位：Cytoplasm. Nucleus.
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蛋白家族：DDB1 family
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