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AB114333

Recombinant Human DDB1 protein (GST tag N-Terminus)

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(2 Publications)

Recombinant Human DDB1 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 1140 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

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

1 Images
SDS-PAGE - Recombinant Human DDB1 protein (GST tag N-Terminus) (AB114333)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human DDB1 protein (GST tag N-Terminus) (AB114333)

ab114333 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

SDS-PAGE, ELISA, WB

applications

Biologically active

No

Accession

Q16531

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"154 kDa","actualMolecularWeight":null,"aminoAcidEnd":1140,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q16531","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

Specifications

Form

Liquid

General info

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 (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).

Sequence similarities

Belongs to the DDB1 family.

Post-translational modifications

Phosphorylated by ABL1.. Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis.. Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238). Deacetylation by SIRT7 impairs the interaction with CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238).

Product protocols

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 (2)

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

Acta pharmaceutica Sinica. B 14:4001-4013 PubMed39309493

2024

Molecular glue triggers degradation of PHGDH by enhancing the interaction between DDB1 and PHGDH.

Applications

Unspecified application

Species

Unspecified reactive species

Ziqi Huang,Kun Zhang,Yurui Jiang,Mengmeng Wang,Mei Li,Yuda Guo,Ruolin Gao,Ning Li,Chenyang Wang,Jia Chen,Jiefu Wang,Ning Liu,Xiang Liu,Shuangwei Liu,Mingming Wei,Cheng Yang,Guang Yang

Cell reports 29:3620-3635.e7 PubMed31825840

2019

Raptor-Mediated Proteasomal Degradation of Deamidated 4E-BP2 Regulates Postnatal Neuronal Translation and NF-κB Activity.

Applications

Unspecified application

Species

Unspecified reactive species

Stella Kouloulia,Erik I Hallin,Konstanze Simbriger,Inês S Amorim,Gilliard Lach,Theoklitos Amvrosiadis,Kleanthi Chalkiadaki,Agniete Kampaite,Vinh Tai Truong,Mehdi Hooshmandi,Seyed Mehdi Jafarnejad,Paul Skehel,Petri Kursula,Arkady Khoutorsky,Christos G Gkogkas
View all publications

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