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Validated All-in-One™ qPCR Primer for DDB2(NM_000107.2) Search again
Product ID:
HQP004114
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
DDBB, UV-DDB2, XPE
Gene Description:
damage specific DNA binding protein 2
Target Gene Accession:
NM_000107.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a protein that is necessary for the repair of ultraviolet light-damaged DNA. This protein is the smaller subunit of a heterodimeric protein complex that participates in nucleotide excision repair, and this complex mediates the ubiquitylation of histones H3 and H4, which facilitates the cellular response to DNA damage. This subunit appears to be required for DNA binding. Mutations in this gene cause xeroderma pigmentosum complementation group E, a recessive disease that is characterized by an increased sensitivity to UV light and a high predisposition for skin cancer development, in some cases accompanied by neurological abnormalities. [provided by RefSeq].
Gene References into function
- These results indicate that DDB2 is a modulator of UV-induced apoptosis, and that UV resistance can be overcome by inhibition of DDB2
- These results demonstrate direct activation of the human DDB2 gene by p53. The corresponding region in the mouse DDB2 gene shared significant sequence identity with the human gene but was deficient for p53 binding and transcriptional activation.
- Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation
- 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
- 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.
- BRCA1 upregulates DDB2, with some evidence that p53 is involved in its regulation.
- overexpression of DDB2 in V79 cell potentiates DNA repair and protects cells from UV-induced apoptosis and cytotoxicity.
- DDB2 and CSA are each integrated into nearly identical complexes via interaction with DDB1
- DDB2p48 activates the recruitment of XPC to cyclobutane pyrimidine dimers and may be the initial recognition factor in the nucleotide excision repair pathway
- Data suggest that both before and after UV irradiation, DDB2 directly regulates p53 levels, while DDB2 expression is itself regulated by p53.
- identification of four DDB2 variants from HeLa cells (D1-D4) that are generated by alternative splicing
- DDB2 regulates TNF signaling-mediated apoptosis via cFLIP and contributes to acquired cross-resistance.
- UV-DDB interacts with XPC physically, and both are polyubiquitylated by the UV-DDB-ubiquitin ligase complex.
- DDB1-DDB2 protein complex recognizes DNA mismatches and lesions
- DDB2 has an intrinsic damaged DNA binding activity
- Monoubiquitinated histone H2A in native chromatin coimmunoprecipitates with the endogenous DDB1-CUL4A(DDB2) complex in response to UV irradiation.
- CUL-4A mediates the proteolytic degradation of DDB2 and this degradation event, initiated at the lesion sites, regulates damage recognition by XPC.
- DDB2 can bind to damaged DNA in vivo as a monomer, whereas Cul4A recruitment to damage sites depends on the fully assembled complex.
- Results suggest that the roles of p53 and nucleotide excision repair in the recovery from UV-induced replication are separable and DDB2-independent.
- A nonsense mutation 574CT (R192X) in DDB2 was found in association facial neoplasms in a form of xeroderma pigmentosum.The parents were heterozygous & the patient homozygous.
- provide genetic evidence linking the regulation of p21(Waf1/Cip1) to the nucleotide excision repair activity of DDB2
- p53 determines the switch by regulating ddb2 and DNA double-strand breaks in antineoplastic agent treatment of glioblastoma multiforme.
- These findings demonstrate for the first time that DDB2 can play a role as oncogene and may become a promising candidate as a predictive marker in breast cancer.
- DDB1-CUL4B(DDB2) E3 ligase may have a distinctive function in modifying the chromatin structure at the site of UV lesions to promote efficient NER.
- p38 MAPK regulates chromatin remodeling as well as DDB2 degradation for facilitating NER factor assembly
- Results suggest a model in which UV-dependent degradation of DDB2 is important for the release of DDB1 from continuous association to unrepaired DNA and makes DDB1 available for its other DNA damage response functions.
- The structure DDB1-DDB2 complex shows the tightly localized probing of the photolesions, combined with proofreading in the photodimer pocket, enables DDB2 to detect lesions refractory to detection by other damage surveillance proteins.