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AB9194

Anti-DDB1 antibody

4

(2 Reviews)

|

(13 Publications)

Goat Polyclonal DDB1 antibody. Suitable for IHC-P, WB and reacts with Human, Mouse samples. Cited in 13 publications. Immunogen corresponding to Synthetic Peptide within Human DDB1 aa 1100 to C-terminus.

View Alternative Names

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

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DDB1 antibody (AB9194)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DDB1 antibody (AB9194)

Left panel : Immunohistochemical analysis of paraffin-embedded human cortex tissue labelling DDB1 with ab9194 at 4μg/ml. Heat mediated antigen retrieval with citrate buffer pH 6, HRP-staining.

Right panel : Immunohistochemical analysis of paraffin-embedded human cortex tissue with no primary antibody.

Western blot - Anti-DDB1 antibody (AB9194)
  • WB

Supplier Data

Western blot - Anti-DDB1 antibody (AB9194)

Primary incubation for 1 hour. Detected by chemiluminescence. RIPA buffer used.

All lanes:

Western blot - Anti-DDB1 antibody (ab9194) at 1 µg/mL

Lane 1:

HeLa (Human cervix adenocarcinoma epithelial cell) whole cell lysate at 35 µg

Lane 2:

Hep G2 (Human liver hepatocellular carcinoma cell line) whole cell lysate at 35 µg

Lane 3:

Jurkat (Human T cell leukemia cell line from peripheral blood) whole cell lysate at 35 µg

Predicted band size: 127 kDa

Observed band size: 140 kDa

false

Western blot - Anti-DDB1 antibody (AB9194)
  • WB

Supplier Data

Western blot - Anti-DDB1 antibody (AB9194)

Primary incubation for 1 hour. Detected by chemiluminescence. RIPA buffer used.

All lanes:

Western blot - Anti-DDB1 antibody (ab9194) at 0.01 µg/mL

Lane 1:

NIH/3T3 (Mouse embryonic fibroblast cell line) whole cell lysate at 35 µg

Lane 2:

NSO (Murine myeloma cells) whole cell lysate at 35 µg

Predicted band size: 127 kDa

Observed band size: 140 kDa,150 kDa

false

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Mouse

Applications

WB, IHC-P

applications

Immunogen

Synthetic Peptide within Human DDB1 aa 1100 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q16531

Reactivity data

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Product details

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

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: Tris buffered saline, 0.5% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

DDB1 also known as Damage-Specific DNA Binding Protein 1 and DDB00A acts mechanically by recognizing and binding to DNA damage sites particularly UV-induced lesions. It functions as part of the UV-damaged DNA-binding protein complex. DDB1 has a molecular weight of approximately 127 kDa. It expresses in various tissues prominently in cells that are actively cycling. The protein often cooperates with other proteins to promote DNA repair and maintenance of genomic stability.
Biological function summary

In terms of cellular processes beyond DDB1's immediate interactions it plays a critical role in DNA repair mechanisms and the cell cycle. DDB1 is part of the larger CUL4-DDB1 ubiquitin ligase complex which targets specific proteins for ubiquitination and subsequent degradation therefore facilitating DNA repair and regulating cell cycle progression. This ability to target damaged proteins or signaling errors for removal helps maintain cellular health and preserve genetic information integrity.

Pathways

DDB1 is pivotal in the nucleotide excision repair pathway and the DNA damage response pathway. It interacts dynamically with proteins such as XPC (xeroderma pigmentosum group C) to initiate repair mechanisms ensuring the proper removal of damaged DNA sections. Moreover DDB1's role in ubiquitination connects it to pathways regulating protein turnover and cellular homeostasis interacting with the ubiquitin-proteasome system which is important for controlling protein degradation.

DDB1's malfunction or misregulation associates with conditions like xeroderma pigmentosum due to its role in DNA damage repair. It is also linked to certain cancer types where DNA repair deficiencies contribute to uncontrolled cell proliferation. Through these diseases DDB1 often interacts with proteins such as BRWD3 which may modulate DDB1's activity or stability influencing the disease outcomes by affecting the DNA repair capacity or recognizing specific proteins for degradation.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

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

Publications (13)

Recent publications for all applications. Explore the full list and refine your search

iScience 27:108933 PubMed38318354

2024

Cullin-RING E3 ubiquitin ligase 4 regulates neurite morphogenesis during neurodevelopment.

Applications

Unspecified application

Species

Unspecified reactive species

Tammy Shim,Jae Yeon Kim,WonCheol Kim,Yun-Il Lee,Bongki Cho,Cheil Moon

iScience 24:103093 PubMed34622148

2021

Ezh2 harnesses the intranuclear actin cytoskeleton to remodel chromatin in differentiating Th cells.

Applications

Unspecified application

Species

Unspecified reactive species

Moran Titelbaum,Boris Brant,Daniel Baumel,Alina Burstein-Willensky,Shira Perez,Yiftah Barsheshet,Orly Avni

Metabolism: clinical and experimental 107:154222 PubMed32246987

2020

DDB1 E3 ligase controls dietary fructose-induced ChREBPα stabilization and liver steatosis via CRY1.

Applications

Unspecified application

Species

Unspecified reactive species

Xin Tong,Deqiang Zhang,Omar Shabandri,Joon Oh,Ethan Jin,Kenneth Stamper,Meichan Yang,Zifeng Zhao,Lei Yin

International journal of biological sciences 16:1059-1070 PubMed32140073

2020

Small molecule NSC1892 targets the CUL4A/4B-DDB1 interactions and causes impairment of CRL4 E3 ligases to inhibit colorectal cancer cell growth.

Applications

Unspecified application

Species

Unspecified reactive species

Chunmei Yang,Jing Wu,Hongbo He,Hong Liu

PLoS genetics 15:e1007685 PubMed30779731

2019

Cul4-Ddb1 ubiquitin ligases facilitate DNA replication-coupled sister chromatid cohesion through regulation of cohesin acetyltransferase Esco2.

Applications

Unspecified application

Species

Unspecified reactive species

Haitao Sun,Jiaxin Zhang,Siyu Xin,Meiqian Jiang,Jingjing Zhang,Zhen Li,Qinhong Cao,Huiqiang Lou

Nature communications 9:1040 PubMed29531219

2018

TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A.

Applications

WB

Species

Unspecified reactive species

Alex Pines,Madelon Dijk,Matthew Makowski,Elisabeth M Meulenbroek,Mischa G Vrouwe,Yana van der Weegen,Marijke Baltissen,Pim J French,Martin E van Royen,Martijn S Luijsterburg,Leon H Mullenders,Michiel Vermeulen,Wim Vermeulen,Navraj S Pannu,Haico van Attikum

The Journal of cell biology 199:235-49 PubMed23045548

2012

PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1.

Applications

WB

Species

Unspecified reactive species

Alex Pines,Mischa G Vrouwe,Jurgen A Marteijn,Dimitris Typas,Martijn S Luijsterburg,Medine Cansoy,Paul Hensbergen,André Deelder,Anton de Groot,Syota Matsumoto,Kaoru Sugasawa,Nicolas Thoma,Wim Vermeulen,Harry Vrieling,Leon Mullenders

Skeletal muscle 1:15 PubMed21798095

2011

Deregulation of the ubiquitin-proteasome system is the predominant molecular pathology in OPMD animal models and patients.

Applications

ICC/IF

Species

Mouse

Seyed Yahya Anvar,Peter Ac 't Hoen,Andrea Venema,Barbara van der Sluijs,Baziel van Engelen,Marc Snoeck,John Vissing,Capucine Trollet,George Dickson,Aymeric Chartier,Martine Simonelig,Gert-Jan B van Ommen,Silvere M van der Maarel,Vered Raz

Cancer research 69:2630-7 PubMed19276361

2009

DDB1 targets Chk1 to the Cul4 E3 ligase complex in normal cycling cells and in cells experiencing replication stress.

Applications

WB

Species

Human

Van Leung-Pineda,Jiwon Huh,Helen Piwnica-Worms

Molecular and cellular biology 28:7402-13 PubMed18936169

2008

Cellular concentrations of DDB2 regulate dynamic binding of DDB1 at UV-induced DNA damage.

Applications

WB, ICC/IF

Species

Mouse, Mouse

Sergey Alekseev,Martijn S Luijsterburg,Alex Pines,Bart Geverts,Pierre-Olivier Mari,Giuseppina Giglia-Mari,Hannes Lans,Adriaan B Houtsmuller,Leon H F Mullenders,Jan H J Hoeijmakers,Wim Vermeulen
View all publications

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