Anti-DDB1 antibody,Abcam,AB9194
Recognizes the large subunit of DNA damage-binding protein - functions in nucleotide-excision repair. Its defective activity causes the repair defect in the patients with xeroderma pigmentosum complementation group E (XPE). DDB-1 (damage-specific DNA binding protein 1) is also known as: DDBA; XAP1; XPCE; XPE-BF;UV-DDB1
Host
Goat
Reactivity
Human, Mouse
Application
WB, IHC-P
Platform ID
BAB779160290

Abcam
Contact
Tel: +44 (0)1223 696000
Fax: +44 (0)1223 215 215
Email:
Specifications
Scientific Background
Target data 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 (PubMed : 14739464, PubMed : 15448697, PubMed : 16260596, PubMed : 16407242, PubMed : 16407252, PubMed : 16482215, PubMed : 16940174, PubMed : 17079684). 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 (PubMed : 15448697, PubMed : 16260596, PubMed : 16407242, PubMed : 16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed : 15448697, PubMed : 16260596, PubMed : 16407242, PubMed : 16940174). 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 (PubMed : 14739464, PubMed : 16407252, PubMed : 16482215, PubMed : 17079684, PubMed : 18332868, PubMed : 18381890, PubMed : 19966799, PubMed : 22118460, PubMed : 25043012, PubMed : 25108355, PubMed : 28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed : 14739464, PubMed : 16407252, PubMed : 16482215, PubMed : 17079684, PubMed : 18332868, PubMed : 18381890, PubMed : 19966799, PubMed : 22118460, PubMed : 25043012, PubMed : 25108355). 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 (PubMed : 16473935, PubMed : 16678110, PubMed : 17041588, PubMed : 18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed : 16473935, PubMed : 16678110, PubMed : 17041588, PubMed : 18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed : 15882621). 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 (PubMed : 17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed : 12732143). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed : 26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity). See full target information DDB1
Category Paths
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