Recombinant Human Dna Repair Protein Complementing Xp-C Cells (XPC) Protein (His)

Name: Recombinant Human Dna Repair Protein Complementing Xp-C Cells (XPC) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03121P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) XPC.

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Dna Repair Protein Complementing Xp-C Cells (XPC) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q01831
Target Symbol	XPC
Synonyms	DNA repair protein complementing XP C cells; DNA repair protein complementing XP-C cells; DNA repair protein complementing XPC cells; p125; RAD4; Xeroderma pigmentosum complementation group C; Xeroderma pigmentosum group C complementing protein; Xeroderma pigmentosum group C protein; Xeroderma pigmentosum group C-complementing protein; Xeroderma pigmentosum group III; XP 3; XP C; XP group C; XP3; Xpc; XPC gene; XPC_HUMAN; XPCC
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SLPAASSSSSSSKRGKKMCSDGEKAEKRSIAGIDQWLEVFCEQEEKWVCVDCVHGVVGQPLTCYKYATKPMTYVVGIDSDGWVRDVTQRYDPVWMTVTRKCRVDAEWWAETLRPYQSPFMDREKKEDLEFQAKHMDQPLPTAIGLYKNHPLYALKRHLLKYEAIYPETAAILGYCRGEAVYSRDCVHTLHSRDTWLKKARVVRLGEVPYKMVKGFSNRARKARLAEPQLREENDLGLFG
Expression Range	496-734aa
Protein Length	Partial
Mol. Weight	31.5kDa
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	Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.; In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes.
Subcellular Location	Nucleus. Chromosome. Cytoplasm.
Protein Families	XPC family
Database References	HGNC: 12816 OMIM: 278720 KEGG: hsa:7508 STRING: 9606.ENSP00000285021 UniGene: PMID: 29973595 CC genotype for XPC A>C polymorphism is associated with the risk of squamous cell carcinoma head and neck. PMID: 29893334 Results show that XPC deficiency leads to alterations in mitochondrial redox balance with a respiratory complex CI/CII shift as a possible adaptation to lower CI activity, but at the cost of sensitizing XP-C cells to mitochondrial oxidative stress. PMID: 28273955 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 Demethylation using decitabine increased XPC and apoptosis after sequential carboplatin. These results confirm that sequential decitabine and carboplatin requires further investigation as a combination treatment for melanoma. PMID: 29373959 These findings support that loss of XPC, possibly due to chronic Cigarette smoke exposure, promotes emphysema development and further supports a link between DNA damage, impaired DNA repair, and development of emphysema. PMID: 29111769 Poly(ADP-ribose) polymerase-1 (PARP1) interacts with xeroderma pigmentosum, complementation group C protein (XPC) in the nucleoplasmic and chromatin fractions in UV irradiated HEK293 cells. PMID: 28760956 hospital workers as a category are at risk for genotoxic damage caused by chronic exposure to xenobiotics. The higher levels of cytogenetic damage observed among GSTT1 null, XPD 751 and XPC 939 CC homozygote subjects confirm the importance of the genetic polymorphisms analysis associated to genotoxicological studies. PMID: 28434254 XPC Ala499Val substitution increases urinary bladder cancer risk, but Lys939Gln appears to be neutral. (Meta-analysis) PMID: 27246180 low XPC and global genome repair have roles in reduced repair of UVB-induced DNA damage in melanoma PMID: 27487145 Several mutations in the two parts of the central "crest" of the arrestin molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 interactions with several GPCRs in receptor subtype and functional state-specific manner. PMID: 28473198 these studies found that carriers of the T allele of ERCC1 rs11615, XPC rs2228000 and rs50872, particularly in postmenopausal females, have an increased risk of breast cancer PMID: 27768589 analysis confirms that XP-C patients without increased sun sensitivity develop non-melanoma skin cancers earlier than sun-sensitive XP-C patients. Reduced cellular mRNA levels are characteristic for XP complementation group C and qRT-PCR represents a rapid diagnostic tool. PMID: 27387384 Data suggest that a common TFIIH subunit p62 recruitment mechanism is shared by UV-stimulated scaffold protein A (UVSSA) in transcription-coupled repair (TCR) and xeroderma pigmentosum, complementation group C protein (XPC) in global genome repair (GGR). PMID: 29069470 CHD1 facilitates substrate handover from XPC to the downstream TFIIH (transcription factor IIH). PMID: 29018037 results provide insights into an unexpected biological role of XPC in response to DNA replication stress PMID: 27794614 Allelic variants in the gene XPC are not associated with an increased risk for developing pre-senile cataract PMID: 27248495 XPC dissociation from the damage site could become a rate-limiting step in nucleotide excision repair (NER) of certain types of DNA adducts, leading to repression of NER. PMID: 27327897 Histone deacetylation plays a significant role in the process of DNA damage recognition for nucleotide excision repair and the localization and functions of XPC can be regulated by acetylated states of histones. PMID: 28233440 The risk of esophageal squamous cell carcinoma associated with XPC rs-2228000 was determined. A homozygous minor allele showed strong association with ESCC risk, especially in smokers, those in adobe houses, and drinkers of salt tea. Variant genotypes of both XPA and XPC in combination showed an increased risk towards ESCC. PMID: 26831662 the associations between three XPC gene polymorphisms (rs2228001 A>C, rs2228000 C>T, and rs2229090 G>C) and neuroblastoma risk with 256 neuroblastoma patients and 531 healthy controls in a Chinese Han population, were investigated. PMID: 27847809 XPC polymorphisms are associated with gastric cancer and atrophic gastritis risks. PMID: 26760766 A chirality change in XPC- and Sfi1-derived peptides affects their affinity for centrin. PMID: 26923803 XPC intron11 C/A polymorphism was associated with an increased risk of prostate cancer. Among non-smokers, the A/A genotype was significantly more prevalent in prostate cancer patients than in controls. PMID: 26745975 No association between XPC polymorphisms and grades/stages of tumors, but report significant association between XPC PAT and reduction of prostate cancer risk in this group of patients. PMID: 27468562 Structural insight into the mechanism of TFIIH recognition by the acidic string of the nucleotide excision repair factor XPC has been uncovered. PMID: 26278177 the present study demonstrates a novel mutation in the XPC gene that may be affecting mRNA synthesis with milder phenotypes. PMID: 26227012 XPC gene Lys939Gln polymorphism is significantly associated with increased risk of mitral chordae tendineae rupture. PMID: 26604426 eIF3a improves ovarian cancer patients' response to cisplatin-based chemotherapy by down regulating XPC and p27(Kip1). PMID: 26213845 Missense mutations in the XPC gene may allow partial functionality that could explain this unusual late onset XP. Atypical clinical presentation of XPC could be misdiagnosed when genetic aberrations allow partial DNA repair capacity. PMID: 26278556 A novel role for the XPC protein in regulating APE1 and OGG1 expression and activity: XPC protein interacts physically with APE1 but not with OGG1.XPC is required for OGG1 activity. PMID: 26811994 XPC's function in DNA quality surveillance preventing sunlight-induced skin cancer is discussed. [review] PMID: 26521083 These data suggest that RNF111, together with the CRL4(DDB2) ubiquitin ligase complex, is responsible for sequential XPC ubiquitylation, which regulates the recruitment and release of XPC and is crucial for efficient progression of the NER reaction. PMID: 26151477 Data show increased risk of leukemia with XPCC protein (XPC) 939Gln/Gln genotype, ERCC2 protein (XPD) 751Gln allele may be protective against chronic myeloid leukemia and acute myeloid leukemia, and no significant risk for the ERCC5 protein (XPG) gene. PMID: 25311495 Attenuated XPC protein expression levels are not associated with genome nucleotide excision repair activity in in bladder cancer. PMID: 25927440 Single Nucleotide Polymorphism in XPC, XPD, XRCC1, and XRCC3 were associated with risk for head and neck squamous cell carcinomas. PMID: 26001739 SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair PMID: 26042670 XPF and XPC expression may be a potential predictive factor for bladder cancer, and smoking can not only influence the recurrence of bladder cancer as a single factor but also aggravate the results of the XPF defect and XPC defect. PMID: 25535740 Data show that nucleotide excision repair factor XPC-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1). PMID: 26170451 Our results confirmed that polymorphisms in XPC and XPD may be associated with the risk of colorectal cancer. PMID: 25391773 Testing of the XPC gene in two families with four xeroderma pigmentosum affected children led to the identification of the novel mutations c.1243C>T or p.R415X and c.1677C>A or p.Y559X. PMID: 25566891 Review/Meta-analysis: XPC polymorphisms were not risk factors for the development of colorectal cancer. PMID: 26214629 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 This meta-analysis suggests that the XPC is a candidate gene for colorectal cancer susceptibility. PMID: 24947936 XPC single nucleotide polymorphism and gene frequency in Russians, Tatars and Bashkirs. PMID: 25474887 we found that Gln939Gln genotype was associated with significantly increased risk of lung cancer in Asian population. PMID: 24736739 Review-Meta-analysis: XPC polymorphisms (Lys939Gln, Val499Arg, and PAT-/+) do not contribute to gastric cancer risk. PMID: 24886180 Chromatin retention of DNA damage sensors DDB2 and XPC through loss of p97 segregase causes genotoxicity. PMID: 24770583 The XPG rs17655 CC genotype is associated with shorter overall survival in gastric cancer. PMID: 24990617 XPC genetic polymorphism is associated with the development of colorectal cancer. PMID: 23803084

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.