Product Details

Uniprot No.

Target Names

Alternative Names

DNA damage-binding protein 1 (DDB p127 subunit) (DNA damage-binding protein a) (DDBa) (Damage-specific DNA-binding protein 1) (HBV X-associated protein 1) (XAP-1) (UV-damaged DNA-binding factor) (UV-damaged DNA-binding protein 1) (UV-DDB 1) (XPE-binding factor) (XPE-BF) (Xeroderma pigmentosum group E-complementing protein) (XPCe), DDB1, XAP1

Species Reactivity

Human, Mouse

Immunogen

Recombinant Antibody

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

6E2

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, WB, IHC

Recommended Dilution

Application	Recommended Dilution
WB	1:500-1:5000
IHC	1:50-1:200

Protocols

ELISA Protocol
Western Blotting(WB) Protocol
Immunohistochemistry (IHC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

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

Lead Time

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.

Description

DDB1 (DNA damage-binding protein 1) serves as a critical scaffold protein within the CUL4-DDB1 ubiquitin ligase complex, playing essential roles in nucleotide excision repair, DNA replication, and cell cycle regulation. As a key component of the UV-damaged DNA-binding factor, DDB1 recognizes and binds to UV-induced DNA lesions, initiating the repair cascade that maintains genomic integrity. Its involvement in multiple cellular processes, including chromatin remodeling and viral protein interactions (notably with hepatitis B virus X protein), makes DDB1 a significant target for cancer biology, DNA repair research, and studies of viral pathogenesis.

This recombinant monoclonal antibody (clone 6E2) offers the reproducibility and consistency that demanding research applications require. Generated against a synthetic peptide derived from human DDB1, the antibody is produced using recombinant technology, ensuring sequence-defined specificity and eliminating the lot-to-lot variability that can compromise longitudinal studies or multi-site collaborations.

Validation studies demonstrate robust performance across multiple experimental platforms. Western blot analysis detects DDB1 at the expected molecular weight range (observed at approximately 130 kDa, slightly higher than the predicted 127 kDa, likely reflecting post-translational modifications such as phosphorylation) across diverse human cell lines including HeLa, A549, HEK293, MCF-7, HT-29, and HepG2, as well as mouse brain tissue, confirming cross-species reactivity. Immunohistochemistry applications have been validated in paraffin-embedded human liver cancer and kidney tissues using citrate buffer antigen retrieval, with recommended dilutions of 1:50–1:200 providing flexibility for optimization across different tissue types.

This antibody is well-suited for researchers investigating DNA damage response pathways, ubiquitin-proteasome regulation, and cancer-associated mechanisms where DDB1 dysfunction contributes to disease progression.

Usage

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

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Target Background

Function

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.

Gene References into Functions

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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Subcellular Location

Cytoplasm. Nucleus.

Protein Families

DDB1 family

Database Links

HGNC: 2717

OMIM: 600045

KEGG: hsa:1642

STRING: 9606.ENSP00000301764

UniGene: Hs.290758

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Code	CSB-RA066000A0HU
Size	US$210
	Order now
Image	Western Blot Positive WB detected in: Hela whole cell lysate(30µg), A549 whole cell lysate(30µg), HEK293 whole cell lysate(30µg), MCF-7 whole cell lysate(30µg), HT-29 whole cell lysate(30µg), HepG2 whole cell lysate(30µg), Mouse brain tissue lysate(30µg) All lanes: DDB1 antibody at 1:1000 Secondary Goat polyclonal to rabbit IgG at 1/40000 dilution Predicted band size: 127 kDa Observed band size: 130 kDa Exposure time：20s IHC image of CSB-RA066000A0HU diluted at 1:100 and staining in paraffin-embedded human liver cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. IHC image of CSB-RA066000A0HU diluted at 1:100 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
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DDB1 Recombinant Monoclonal Antibody

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Target Background