• Call +1.858.633.0165 or Fax +1.858.633.0166 or Contact Us

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

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS960949

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… More details

$315 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
PDF
Sample Manual Insert View PDF
PDF
Testing Data View PDF
PDF
Certificate of Analysis (COA) View PDF
PDF
QC Report View PDF
PDF
Material Safety Data Sheet View PDF
PDF
Technical Datasheet View PDF
PDF
Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
DNA repair protein complementing XP-C cells (XPC), Recombinant Protein
Full Product Name
Recombinant Human DNA repair protein complementing XP-C cells
Product Gene Name
Product Synonym Names
Xeroderma pigmentosum group C-complementing proteinp125
Sequence
SLPAASSSSS SSKRGKKMCS DGEKAEKRSI AGIDQWLEVF CEQEEKWVCV DCVHGVVGQP LTCYKYATKP MTYVVGIDSD GWVRDVTQRY DPVWMTVTRK CRVDAEWWAE TLRPYQSPFM DREKKEDLEF QAKHMDQPLP TAIGLYKNHP LYALKRHLLK YEAIYPETAA ILGYCRGEAV YSRDCVHTLH SRDTWLKKAR VVRLGEVPYK MVKGFSNRAR KARLAEPQLR EENDLGLFG
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
31.5 kDa
Sequence Positions
496-734aa; Partial
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
278720
3D Structure
ModBase 3D Structure for Q01831
Production Note
Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to support@mybiosource.com for more details.
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for XPC recombinant protein

Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23.Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D., Hoeijmakers J.H.J., Hanaoka F.EMBO J. 13:1831-1843(1994) The human XPC DNA repair gene arrangement, splice site information content and influence of a single nucleotide polymorphism in a splice acceptor site on alternative splicing and function.Khan S.G., Muniz-Medina V., Shahlavi T., Baker C.C., Inui H., Ueda T., Emmert S., Schneider T.D., Kraemer K.H.Nucleic Acids Res. 30:3624-3631(2002) Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism.Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.Nat. Commun. 5:3650-3650(2014) NIEHS SNPs programComplete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence, annotation and analysis of human chromosome 3.Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.Nature 440:1194-1198(2006) Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Expression cloning of a human DNA repair gene involved in Xeroderma pigmentosum group C.Legerski R.J., Peterson C.A.Nature 359:70-73(1992) ErratumLegerski R.J., Peterson C.A.Nature 360:610-610(1992) XPC and human homologs of RAD23 intracellular localization and relationship to other nucleotide excision repair complexes.van der Spek P.J., Eker A., Rademakers S., Visser C., Sugasawa K., Masutani C., Hanaoka F., Bootsma D., Hoeijmakers J.H.Nucleic Acids Res. 24:2551-2559(1996) Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity.Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A., van der Spek P.J., Eker A.P., Rademakers S., Visser C., Aboussekhra A., Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H.Mol. Cell. Biol. 17:6924-6931(1997) Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair.Sugasawa K., Ng J.M., Masutani C., Iwai S., van der Spek P.J., Eker A.P., Hanaoka F., Bootsma D., Hoeijmakers J.H.Mol. Cell 2:223-232(1998) The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA.Yokoi M., Masutani C., Maekawa T., Sugasawa K., Ohkuma Y., Hanaoka F.J. Biol. Chem. 275:9870-9875(2000) Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites.Batty D., Rapic'-Otrin V., Levine A.S., Wood R.D.J. Mol. Biol. 300:275-290(2000) Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair.Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F.J. Biol. Chem. 276:18665-18672(2001) A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex.Sugasawa K., Shimizu Y., Iwai S., Hanaoka F.DNA Repair 1:95-107(2002) The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH.Uchida A., Sugasawa K., Masutani C., Dohmae N., Araki M., Yokoi M., Ohkuma Y., Hanaoka F.DNA Repair 1:449-461(2002) DNA bending by the human damage recognition complex XPC-HR23B.Janicijevic A., Sugasawa K., Shimizu Y., Hanaoka F., Wijgers N., Djurica M., Hoeijmakers J.H., Wyman C.DNA Repair 2:325-336(2003) Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase.Shimizu Y., Iwai S., Hanaoka F., Sugasawa K.EMBO J. 22:164-173(2003) UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex.Sugasawa K., Okuda Y., Saijo M., Nishi R., Matsuda N., Chu G., Mori T., Iwai S., Tanaka K., Tanaka K., Hanaoka F.Cell 121:387-400(2005) Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C., Sugasawa K., Hanaoka F.Mol. Cell. Biol. 25:5664-5674(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Toward a global characterization of the phosphoproteome in prostate cancer cells identification of phosphoproteins in the LNCaP cell line.Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.Electrophoresis 28:2027-2034(2007) ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.Science 316:1160-1166(2007) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.Proteomics 8:1346-1361(2008) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation.Yasuda G., Nishi R., Watanabe E., Mori T., Iwai S., Orioli D., Stefanini M., Hanaoka F., Sugasawa K.Mol. Cell. Biol. 27:6606-6614(2007) An aromatic sensor with aversion to damaged strands confers versatility to DNA repair.Maillard O., Solyom S., Naegeli H.PLoS Biol. 5:E79-E79(2007) Versatile DNA damage detection by the global genome nucleotide excision repair protein XPC.Hoogstraten D., Bergink S., Ng J.M., Verbiest V.H., Luijsterburg M.S., Geverts B., Raams A., Dinant C., Hoeijmakers J.H., Vermeulen W., Houtsmuller A.B.J. Cell Sci. 121:2850-2859(2008) ErratumHoogstraten D., Bergink S., Ng J.M., Verbiest V.H., Luijsterburg M.S., Geverts B., Raams A., Dinant C., Hoeijmakers J.H., Vermeulen W., Houtsmuller A.B.J. Cell Sci. 121:2972-2972(2008) ErratumHoogstraten D., Bergink S., Ng J.M., Verbiest V.H., Luijsterburg M.S., Geverts B., Raams A., Dinant C., Hoeijmakers J.H., Vermeulen W., Houtsmuller A.B.J. Cell Sci. 121:3991-3991(2008) Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein.Camenisch U., Trautlein D., Clement F.C., Fei J., Leitenstorfer A., Ferrando-May E., Naegeli H.EMBO J. 28:2387-2399(2009) Two-step recognition of DNA damage for mammalian nucleotide excision repair Directional binding of the XPC complex and DNA strand scanning.Sugasawa K., Akagi J., Nishi R., Iwai S., Hanaoka F.Mol. Cell 36:642-653(2009) Dissection of the xeroderma pigmentosum group C protein function by site-directed mutagenesis.Clement F.C., Kaczmarek N., Mathieu N., Tomas M., Leitenstorfer A., Ferrando-May E., Naegeli H.Antioxid. Redox Signal. 14:2479-2490(2011) Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct.Neher T.M., Rechkunova N.I., Lavrik O.I., Turchi J.J.Biochemistry 49:669-678(2010) Stimulation of DNA glycosylase activities by XPC Protein Complex Roles of protein-protein interactions.Shimizu Y., Uchimura Y., Dohmae N., Saitoh H., Hanaoka F., Sugasawa K.J. Nucleic Acids 2010:455-459(2010) Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair.Yang A., Miron S., Mouawad L., Duchambon P., Blouquit Y., Craescu C.T.Biochemistry 45:3653-3663(2006) The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.Thompson J.R., Ryan Z.C., Salisbury J.L., Kumar R.J. Biol. Chem. 281:18746-18752(2006) Structural, thermodynamic, and cellular characterization of human centrin 2 interaction with xeroderma pigmentosum group C protein.Charbonnier J.B., Renaud E., Miron S., Le Du M.H., Blouquit Y., Duchambon P., Christova P., Shosheva A., Rose T., Angulo J.F., Craescu C.T.J. Mol. Biol. 373:1032-1046(2007) A summary of mutations in the UV-sensitive disorders xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy.Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.3.0.CO;2-6>Hum. Mutat. 14:9-22(1999) Characterization of molecular defects in Xeroderma pigmentosum group C.Li L., Bales E.S., Peterson C.A., Legerski R.J.Nat. Genet. 5:413-417(1993) Mutations in the XPC gene in families with xeroderma pigmentosum and consequences at the cell, protein, and transcript levels.Chavanne F., Broughton B.C., Pietra D., Nardo T., Browitt A., Lehmann A.R., Stefanini M.Cancer Res. 60:1974-1982(2000) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of XPC recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for XPC purchase

MBS960949 is a recombinant protein targeting XPC. Also known as Recombinant Human DNA repair protein complementing XP-C cells. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for XPC. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
DNA repair protein complementing XP-C cells
NCBI Official Synonym Full Names
xeroderma pigmentosum, complementation group C
NCBI Official Symbol
XPC
NCBI Official Synonym Symbols
XP3; RAD4; XPCC; p125
UniProt Protein Name
DNA repair protein complementing XP-C cells
UniProt Synonym Protein Names
Xeroderma pigmentosum group C-complementing protein; p125
Protein Family
UniProt Gene Name
XPC
UniProt Synonym Gene Names
XPCC
UniProt Entry Name
XPC_HUMAN
NCBI Protein Information
DNA repair protein complementing XP-C cells

NCBI Summary for XPC

This gene encodes a component of the nucleotide excision repair (NER) pathway. There are multiple components involved in the NER pathway, including Xeroderma pigmentosum (XP) A-G and V, Cockayne syndrome (CS) A and B, and trichothiodystrophy (TTD) group A, etc. This component, XPC, plays an important role in the early steps of global genome NER, especially in damage recognition, open complex formation, and repair protein complex formation. Mutations in this gene or some other NER components result in Xeroderma pigmentosum, a rare autosomal recessive disorder characterized by increased sensitivity to sunlight with the development of carcinomas at an early age. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2009]
Show more

UniProt Comments for XPC

XPC: a probable nuclear protein involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes. Defects in XPC are a cause of xeroderma pigmentosum complementation group C.

Protein type: DNA repair, damage

Chromosomal Location of Human Ortholog: 3p25.1

Cellular Component: cytoplasm; nucleolus; nucleoplasm; nucleus; plasma membrane

Molecular Function: bubble DNA binding; damaged DNA binding; loop DNA binding; protein binding; single-stranded DNA binding

Biological Process: cellular protein metabolic process; DNA repair; intra-S DNA damage checkpoint; mismatch repair; nucleotide-excision repair; nucleotide-excision repair, DNA damage recognition; post-translational protein modification; protein sumoylation; response to drug; response to UV-B

Disease: Xeroderma Pigmentosum, Complementation Group C
Show more

Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

Request a Quote

Please fill out the form below and our representative will get back to you shortly.

MBS000000
Contact Us

Please fill out the form below and our representative will get back to you shortly.

MBS000000