Recombinant Human Dna Damage-Binding Protein 2 (DDB2) Protein (His)

Name: Recombinant Human Dna Damage-Binding Protein 2 (DDB2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07135P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dna Damage-Binding Protein 2 (DDB2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q92466
Target Symbol	DDB2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGDNVGNVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAACFSPDGARLLTTDQKSEIRVYSASQWDCPLGLIPHPHRHFQHLTPIKAAWHPRYNLIVVGRYPDPNFKSCTPYELRTIDVFDGNSGKMMCQLYDPESSGISSLNEFNPMGDTLASAMGYHILIWSQEEARTRK
Expression Range	1-427aa
Protein Length	Full Length
Mol. Weight	53.8 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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 the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB2-CUL4-ROC1 complex 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. The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR.; Inhibits UV-damaged DNA repair.; Inhibits UV-damaged DNA repair.
Subcellular Location	Nucleus. Note=Accumulates at sites of DNA damage following UV irradiation.
Protein Families	WD repeat DDB2/WDR76 family
Database References	HGNC: 2718 OMIM: 278740 KEGG: hsa:1643 STRING: 9606.ENSP00000256996 UniGene: PMID: 29169765 Chronic low-dose of UVB (CLUV) treatment activates p53, which corroborate with the increased level of DDB2 and XPC proteins. DDB2 and XPC recruited at chromatin bound, suggesting a more efficient cyclobutane pyrimidine dimer (CPD) recognition by NER and more efficient repair of CDP. PMID: 29448173 DDB2-PCNA interaction may contribute to a correct DNA damage response for maintaining genome integrity PMID: 29604309 DDB2 is modified by SUMOylation upon ultraviolet irradiation, and this post-translational modification plays an important role in the initial recognition and processing of ultraviolet irradiation-induced DNA damage occurring within the context of chromatin. PMID: 28981631 Results show that DDB2 is critical for chromatin association of XRCC5/6 in the absence of DNA damage and provide evidence that XRCC5/6 are functional partners of DDB2 in its transcriptional stimulatory activity. PMID: 28035050 UVRAG is a regulator of CRL4(DDB2)-mediated nucleotide excision repair and its expression levels may influence melanoma predisposition. PMID: 27203177 High DDB2 expression is associated with increased radioresistance of non-small cell lung cancer. PMID: 27553023 data revealed that DDB2 is involved in early events occurring during metastatic progression of breast cancer cells and will contribute to define this protein as a new marker of metastatic progression in this type of cancer. PMID: 26879405 DDB2 polymorphisms are associated with gastric cancer and atrophic gastritis risks. PMID: 26760766 the release of NER components such as DNA damage binding protein 2 (DDB2) and Xeroderma Pigmentosum complementation group C protein (XPC) following oxidative stress might putatively involve their apoptotic role rather than DNA repair function. PMID: 26263968 PKM2 interacts with DDB2 and reduces cell survival upon UV irradiation. PMID: 26410533 DDB2 can bind to the promoter region of NEDD4L and recruit enhancer of zeste homolog 2 histone methyltransferase to repress NEDD4L transcription by enhancing histone H3 lysine 27 trimethylation at the NEDD4L promoter. PMID: 26130719 data demonstrated that the DDB2 IRES activity was promoted during stress conditions. These results reveal a novel mechanism contributing to DDB2 expression PMID: 26187069 DDB2 is involved in ubiquitination and degradation of PAQR3 in gastric cancer cells. PMID: 26205499 DDB2 rs747650 is involved in androgen metabolism, inflammation processes and scar formation in severe acne. PMID: 24399259 DDB2 plays an instrumental role in DNA damage induced ROS accumulation, ROS induced premature senescence and inhibition of skin tumorigenesis. PMID: 23109835 DDB2 is protected by XPC from ubiquitination and degradation in a stochastic manner; thus XPC allows DDB2 to initiate multiple rounds of repair events, thereby contributing to the persistence of cellular DNA repair capacity PMID: 25628365 DDB2 protein expression is low in ovarian tumor cells. PMID: 24574518 Chromatin retention of DNA damage sensors DDB2 and XPC through loss of p97 segregase causes genotoxicity. PMID: 24770583 DDB2 is a PCNA-binding protein and this association is required for DDB2 proteolytic degradation. PMID: 24200966 study provides new knowledge about the posttranslational regulation of DDB2 and expands the biological functions of protein alpha-N-methylation to DNA repair PMID: 24753253 the data indicate that p53-dependent upregulation of XPC and DDB2 is a key mechanism upon genotoxic stress, whereby melanoma cells acquire resistance towards DNA cross-linking agents. PMID: 23604128 DDB2 and a DDB2-ATM feedback loop influence HCMV replication. PMID: 24335308 Knockdown of DDB2-induced IkappaBalpha gene expression restored NF-kappaB activity. PMID: 23774208 These results suggest that the SUMOylation of DDB2 facilitates CPD repair. PMID: 23860269 DDB2 facilitates ATR and ATM recruitment to the DNA damage site following UV irradiation. PMID: 23422745 Results indicate a transcriptional regulatory pathway of DDB2 that is directly linked to the mechanisms that suppress metastasis of colon cancer. PMID: 23610444 The 3'untranslated region of DDB2 contains a cis-acting element that affects stability, export and translation of the message PMID: 23605047 Data indicate that poly(ADP-ribose) polymerase-1 (PARP-1)collaborates with DNA-binding protein 2 (DDB2) to increase the efficiency of the lesion recognition step of global genomic subpathway of NER (GG-NER). PMID: 23319653 DDB2 can inhibit cell growth rate in AR-expressing cells (LNCaP) but not in AR-null cells (PC3). PMID: 22846800 data support a model in which poly(ADP-ribosyl)ation of DDB2 suppresses DDB2 ubiquitylation and outline a molecular mechanism for PARP1-mediated regulation of nucleotide excision repair through DDB2 stabilization and recruitment of the chromatin remodeler ALC1 PMID: 23045548 study reports a new function of DDB2 in modulating chromatin structure at DNA lesions PMID: 22492724 DDB2 subunit of UV-DDB associates transiently with the DNA-binding domain of XPC to fine-tune its engagement with CPD lesions PMID: 22039351 Nucleotide excision repair proteins rapidly accumulate but fail to persist in human xeroderma pigmentosum XP-E (DDB2 mutant) cells. PMID: 21388382 Multiple skin cancers in adults are associted with mutations in the XP-E (DDB2) DNA repair gene. PMID: 21107348 Overexpression of DDB2 enhances the sensitivity of ovarian cancer cells to cisplatin by augmenting cellular apoptosis. PMID: 20013802 Damaged DNA-binding protein 2 (DDB2) protects against UV irradiation in human cells and Drosophila PMID: 20398405 Data show that XPC and Ku oppositely regulate the ubiquitin ligase activity of DDB2, and that DDB2 complex-mediated ubiquitylation plays a role in recruiting XPA to damaged sites. PMID: 20368362 These results indicate that DDB2 is a modulator of UV-induced apoptosis, and that UV resistance can be overcome by inhibition of DDB2 PMID: 11852074 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. PMID: 11971958 BRCA1 upregulates DDB2, with some evidence that p53 is involved in its regulation. PMID: 12496474 overexpression of DDB2 in V79 cell potentiates DNA repair and protects cells from UV-induced apoptosis and cytotoxicity. PMID: 12553360 DDB2 and CSA are each integrated into nearly identical complexes via interaction with DDB1 PMID: 12732143 DDB2p48 activates the recruitment of XPC to cyclobutane pyrimidine dimers and may be the initial recognition factor in the nucleotide excision repair pathway PMID: 12944386 Data suggest that both before and after UV irradiation, DDB2 directly regulates p53 levels, while DDB2 expression is itself regulated by p53. PMID: 14560002 identification of four DDB2 variants from HeLa cells (D1-D4) that are generated by alternative splicing PMID: 14751237 DDB2 regulates TNF signaling-mediated apoptosis via cFLIP and contributes to acquired cross-resistance. PMID: 15644494 UV-DDB interacts with XPC physically, and both are polyubiquitylated by the UV-DDB-ubiquitin ligase complex. PMID: 15882621 DDB2 has an intrinsic damaged DNA binding activity PMID: 16260596 CUL-4A mediates the proteolytic degradation of DDB2 and this degradation event, initiated at the lesion sites, regulates damage recognition by XPC. PMID: 16527807

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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