Desmoplakin Recombinant Protein | DSP recombinant protein

Recombinant Human Desmoplakin

Cat. Num. AAA949399

• Gene Names: DSP; DP; DCWHKTA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Desmoplakin; Recombinant Human Desmoplakin; 250/210 kDa paraneoplastic pemphigus antigen; DSP recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 78-300. Partial-length
• Sequence: CSDCLMRAELIVQPELKYGDGIQLTRSRELDECFAQANDQMEILDSLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGGGGYTCQSGSGWDEFTKHVTSECLGWMRQQRAEMDMVAWGVDLASVEQHINSHRGIHNSIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSD

• 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 [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for DSP recombinant protein

Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin-plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes.

Product Categories/Family for DSP recombinant protein

Signal Transduction

References

Molecular structure of the human desmoplakin I and II amino terminus.Virata M.L.A., Wagner R.M., Parry D.A.D., Green K.J.Proc. Natl. Acad. Sci. U.S.A. 89:544-548(1992) Identification and characterization of DSPIa, a novel isoform of human desmoplakin.Cabral R.M., Wan H., Cole C.L., Abrams D.J., Kelsell D.P., South A.P.Cell Tissue Res. 341:121-129(2010) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) Structure of the human desmoplakins. Implications for function in the desmosomal plaque.Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M., Angst B.D., Nilles L.A.J. Biol. Chem. 265:2603-2612(1990) ErratumGreen K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M., Angst B.D., Nilles L.A.J. Biol. Chem. 265:11406-11407(1990) Striate palmoplantar keratoderma resulting from desmoplakin haploinsufficiency.Whittock N.V., Ashton G.H., Dopping-Hepenstal P.J., Gratian M.J., Keane F.M., Eady R.A.J., McGrath J.A.J. Invest. Dermatol. 113:940-946(1999) The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes.Kowalczyk A.P., Bornslaeger E.A., Borgwardt J.E., Palka H.L., Dhaliwal A.S., Corcoran C.M., Denning M.F., Green K.J.J. Cell Biol. 139:773-784(1997) Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope.Marekov L.N., Steinert P.M.J. Biol. Chem. 273:17763-17770(1998) Haploinsufficiency of desmoplakin causes a striate subtype of palmoplantar keratoderma.Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J., Leigh I.M., Hughes A.E.Hum. Mol. Genet. 8:143-148(1999) ErratumArmstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J., Leigh I.M., Hughes A.E.Hum. Mol. Genet. 8:943-943(1999) Recessive mutation in desmoplakin disrupts desmoplakin-intermediate filament interactions and causes dilated cardiomyopathy, woolly hair and keratoderma.Norgett E.E., Hatsell S.J., Carvajal-Huerta L., Cabezas J.-C.R., Common J., Purkis P.E., Whittock N.V., Leigh I.M., Stevens H.P., Kelsell D.P.Hum. Mol. Genet. 9:2761-2766(2000) Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly.Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.J. Cell Sci. 116:387-399(2003) Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus.Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L.Mol. Biol. Cell 14:1978-1992(2003) Early death from cardiomyopathy in a family with autosomal dominant striate palmoplantar keratoderma and woolly hair associated with a novel insertion mutation in desmoplakin.Norgett E.E., Lucke T.W., Bowers B., Munro C.S., Leigh I.M., Kelsell D.P.J. Invest. Dermatol. 126:1651-1654(2006) 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) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(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) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) 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) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy caused by desmocollin-2 mutations.Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A., Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C., Saffitz J.E., Protonotarios N., McKenna W.J.Cardiovasc. Res. 90:77-87(2011) A new hypo/oligodontia syndrome Carvajal/Naxos syndrome secondary to desmoplakin-dominant mutations.Chalabreysse L., Senni F., Bruyere P., Aime B., Ollagnier C., Bozio A., Bouvagnet P.J. Dent. Res. 90:58-64(2011) 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) Molecular insights into arrhythmogenic right ventricular cardiomyopathy caused by plakophilin-2 missense mutations.Kirchner F., Schuetz A., Boldt L.H., Martens K., Dittmar G., Haverkamp W., Thierfelder L., Heinemann U., Gerull B.Circ. Cardiovasc. Genet. 5:400-411(2012) 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) Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure.Choi H.J., Park-Snyder S., Pascoe L.T., Green K.J., Weis W.I.Nat. Struct. Biol. 9:612-620(2002) Crystal structure of a rigid four-spectrin-repeat fragment of the human desmoplakin plakin domain.Choi H.J., Weis W.I.J. Mol. Biol. 409:800-812(2011) Mutation in human desmoplakin domain binding to plakoglobin causes a dominant form of arrhythmogenic right ventricular cardiomyopathy.Rampazzo A., Nava A., Malacrida S., Beffagna G., Bauce B., Rossi V., Zimbello R., Simionati B., Basso C., Thiene G., Towbin J.A., Danieli G.A.Am. J. Hum. Genet. 71:1200-1206(2002) Compound heterozygosity for non-sense and mis-sense mutations in desmoplakin underlies skin fragility/woolly hair syndrome.Whittock N.V., Wan H., Morley S.M., Garzon M.C., Kristal L., Hyde P., McLean W.H.I., Pulkkinen L., Uitto J., Christiano A.M., Eady R.A.J., McGrath J.A.J. Invest. Dermatol. 118:232-238(2002) A recessive mutation in desmoplakin causes arrhythmogenic right ventricular dysplasia, skin disorder, and woolly hair.Alcalai R., Metzger S., Rosenheck S., Meiner V., Chajek-Shaul T.J. Am. Coll. Cardiol. 42:319-327(2003) Loss of desmoplakin tail causes lethal acantholytic epidermolysis bullosa.Jonkman M.F., Pasmooij A.M.G., Pasmans S.G.M.A., van den Berg M.P., Ter Horst H.J., Timmer A., Pas H.H.Am. J. Hum. Genet. 77:653-660(2005) Clinical profile of four families with arrhythmogenic right ventricular cardiomyopathy caused by dominant desmoplakin mutations.Bauce B., Basso C., Rampazzo A., Beffagna G., Daliento L., Frigo G., Malacrida S., Settimo L., Danieli G., Thiene G., Nava A.Eur. Heart J. 26:1666-1675(2005) Comprehensive desmosome mutation analysis in North Americans with arrhythmogenic right ventricular dysplasia/cardiomyopathy.den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A., Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D., Bluemke D.A., Calkins H., Dalal D., Judge D.P.Circ. Cardiovasc. Genet. 2:428-435(2009) Role of genetic testing in arrhythmogenic right ventricular cardiomyopathy/dysplasia.Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L., Robb L., Talajic M., Brugada R.Clin. Genet. 77:37-48(2010) Expanding the phenotype associated with a desmoplakin dominant mutation Carvajal/Naxos syndrome associated with leukonychia and oligodontia.Boule S., Fressart V., Laux D., Mallet A., Simon F., de Groote P., Bonnet D., Klug D., Charron P.Int. J. Cardiol. 161:50-52(2012) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 58530842
• NCBI GeneID: 1832
• NCBI Accession #: NP_001008844.1
• NCBI GenBank Nucleotide #: NM_001008844.2
• UniProt Accession #: P15924; O75993; Q14189; Q9UHN4; B2RTT2; D7RX09
• Molecular Weight: 28.1 kDa
• NCBI Official Full Name: desmoplakin isoform II
• NCBI Official Synonym Full Names: desmoplakin
• NCBI Official Symbol: DSP
• NCBI Official Synonym Symbols: DP; DCWHKTA
• NCBI Protein Information: desmoplakin
• UniProt Protein Name: Desmoplakin
• Protein Family: Desmoplakin
• UniProt Gene Name: DSP
• UniProt Synonym Gene Names: DP
• UniProt Entry Name: DESP_HUMAN

NCBI Description

This gene encodes a protein that anchors intermediate filaments to desmosomal plaques and forms an obligate component of functional desmosomes. Mutations in this gene are the cause of several cardiomyopathies and keratodermas, including skin fragility-woolly hair syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]

Uniprot Description

Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin-plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes.