Product nameAnti-DDB1 antibody [EPR6088]
See all DDB1 primary antibodies
DescriptionRabbit monoclonal [EPR6088] to DDB1
Tested applicationsSuitable for: WBmore details
Unsuitable for: Flow Cyt,ICC,IHC-P or IP
Species reactivityReacts with: Mouse, Rat, Human
Synthetic peptide within Human DDB1 aa 50-150. The exact sequence is proprietary.
- HeLa, HepG2, NIH 3T3 and Jurkat cell lysates.
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Dissociation constant (KD)KD = 1.35 x 10 -11 M Learn more about KD
Storage bufferpH: 7.20
Preservative: 0.05% Sodium azide
Constituents: 40% Glycerol, 9.85% Tris glycine, 50% Tissue culture supernatant
PurityTissue culture supernatant
Our Abpromise guarantee covers the use of ab124672 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/10000 - 1/50000. Detects a band of approximately 127 kDa (predicted molecular weight: 127 kDa).|
FunctionRequired for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize 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 appears to function 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). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2.
PathwayProtein modification; protein ubiquitination.
Sequence similaritiesBelongs to the DDB1 family.
modificationsUbiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis.
Cellular localizationCytoplasm. Nucleus. Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage.
- Information by UniProt
- Damage specific DNA binding protein 1 antibody
- Damage-specific DNA-binding protein 1 antibody
- DDB 1 antibody
All lanes : Anti-DDB1 antibody [EPR6088] (ab124672) at 1/10000 dilution
Lane 1 : HeLa cell lysates
Lane 2 : HepG2 cell lysates
Lane 3 : NIH 3T3 cell lysates
Lane 4 : Jurkat cell lysates
Lysates/proteins at 10 µg per lane.
All lanes : Goat anti-Rabbit HRP at 1/2000 dilution
Predicted band size: 127 kDa
Equilibrium disassociation constant (KD)
Learn more about KD
Click here to learn more about KD
This product has been referenced in:
- Romani B et al. HIV-1 Vpr Protein Induces Proteasomal Degradation of Chromatin-associated Class I HDACs to Overcome Latent Infection of Macrophages. J Biol Chem 291:2696-711 (2016). WB ; Human . Read more (PubMed: 26679995) »
- Romani B et al. HIV-1 Vpr Protein Enhances Proteasomal Degradation of MCM10 DNA Replication Factor through the Cul4-DDB1[VprBP] E3 Ubiquitin Ligase to Induce G2/M Cell Cycle Arrest. J Biol Chem 290:17380-9 (2015). Read more (PubMed: 26032416) »