Rat DNA Damage-Binding Protein 1 (DDB1) ELISA Kit
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Description
Rat DNA Damage-Binding Protein 1 (DDB1) ELISA Kit is an ELISA Kit for the in vitro quantitative measurement of Rat DDB1 concentrations in tissue homogenates, cell lysates and other biological fluids.
Documents del producto
Product specifications
| Category | ELISA Kits |
| Immunogen Target | DNA Damage-Binding Protein 1 (DDB1) |
| Reactivity | Rat |
| Detection Method | Colorimetric |
| Assay Data | Quantitative |
| Assay Type | Sandwich |
| Test Range | 0.156 ng/ml - 10 ng/ml |
| Sensitivity | < 0.07 ng/ml |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Size 1 | 96 tests |
| Form | Lyophilized |
| Tested Applications | ELISA |
| Sample Type | Tissue homogenates, cell lysates and other biological fluids. |
| Availability | Shipped within 5-15 working days. The validity for this kit is 6 months. |
| Storage | Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. |
| Dry Ice | No |
| UniProt ID | Q9ESW0 |
| Alias | XPE,DDBA,XAP1,XPCE,XPE-BF,UV-DDB1,WHIKERS,UV-damaged DNA-binding factor,DNA damage-binding protein a,DDB p127 subunit |
| Background | Elisa kits for DDB1 |
| Status | RUO |
| Note | Validity: The validity for this kit is 6 months. This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. |
Descripción
Damage-specific DNA binding protein 1 (DDB1) is a critical component of the ubiquitin-proteasome system, serving as a scaffold protein within the CUL4-DDB1 E3 ubiquitin ligase complex. DDB1 interacts with various substrate receptors, including members of the DCAF (DDB1 and CUL4-associated factors) family, to mediate the recognition and ubiquitination of target proteins. Its role is pivotal in regulating DNA repair, particularly nucleotide excision repair (NER), where it facilitates the removal of UV-induced photoproducts and bulky DNA adducts. DDB1 also contributes to the degradation of proteins involved in transcriptional regulation, cell cycle progression, and genome stability. Structurally, DDB1 contains WD40 domains that mediate interactions with CUL4 and substrate receptors, ensuring versatility and specificity in substrate selection. Dysregulation of DDB1 has been associated with genomic instability and cancer development. Its ubiquitous expression highlights its fundamental role in cellular homeostasis and DNA damage response pathways.
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The protein encoded by this gene is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex while another protein (p48) forms the small subunit. This protein complex functions in nucleotide-excision repair and binds to DNA following UV damage. Defective activity of this complex causes the repair defect in patients with xeroderma pigmentosum complementation group E (XPE) - an autosomal recessive disorder characterized by photosensitivity and early onset of carcinomas. However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform mascular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients. The protein encoded by this gene also functions as an adaptor molecule for the cullin 4 (CUL4) ubiquitin E3 ligase complex by facilitating the binding of substrates to this complex and the ubiquitination of proteins.
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Required 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.
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DDB1 Antibody is a Rabbit Polyclonal antibody against DDB1. The protein encoded by this gene is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex while another protein (p48) forms the small subunit. This protein complex functions in nucleotide-excision repair and binds to DNA following UV damage. Defective activity of this complex causes the repair defect in patients with xeroderma pigmentosum complementation group E (XPE) - an autosomal recessive disorder characterized by photosensitivity and early onset of carcinomas. However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform mascular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients. The protein encoded by this gene also functions as an adaptor molecule for the cullin 4 (CUL4) ubiquitin E3 ligase complex by facilitating the binding of substrates to this complex and the ubiquitination of proteins.
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