DDB-1 Antibody #5428
- WB
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 127 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
DDB-1 Antibody detects endogenous levels of total DDB-1 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human DDB-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Damaged DNA-Binding Protein (DDB) consists of a 127 kDa subunit (DDB-1) and a 48 kDa subunit (DDB-2) that contribute to the formation of the UV-damaged DNA-binding protein complex (UV-DDB) (1-3). In conjunction with CUL4A and ROC-1, the UV-DDB complex forms an E3 ubiquitin ligase that recognizes a broad spectrum of DNA lesions such as cyclobutane pyrimidine dimers, 6-4 photoproducts, apurinic sites and short mismatches. The complex polyubiquitinates components of the nucleotide excision repair pathway (4-6). Loss of DDB activity has been identified in a subset of xeroderma pigmentosum complementation group E (XP-E) patients and has been linked to the deficient repair of cyclobutane pyrimidine dimers in cells derived from these patients (7-10).
DDB-1 is a relatively abundant protein that is vital for normal cell function and is evolutionarily conserved in mammals, insects, worms and plants. Unlike DDB-2, lesions in DDB-1 have yet to be indentified in XP-E patients. In association with ROC-1 and CUL4A, DDB-1 functions to recruit substrate-specific targeting subunits, generally known as DCAFs or CDWs, to CUL4-RING E3 ubiquitin-protein ligase complexes (11,12). Ubiquitination of histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage by the DDB1-DDB2-CUL4A-ROC1 E3 ubiquitin-protein ligase complex may facilitate their removal from the nucleosome in order to promote DNA repair (13-15). DDB-1, in association with other CUL4-based E3 ligase complexes, has also been found to be a regulator of mTOR signaling (16,17).
Limited Uses
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