protein

Recombinant Human Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

MBS960502

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Calcium pump 2; Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform; Endoplasmic reticulum class 1/2 Ca(2+) ATPase

sarcoplasmic/endoplasmic reticulum calcium ATPase 2 isoform a; Sarcoplasmic/endoplasmic reticulum calcium ATPase 2; sarcoplasmic/endoplasmic reticulum calcium ATPase 2; ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 2; Calcium pump 2; Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform; Endoplasmic reticulum class 1/2 Ca(2+) ATPase

ATP2A2

ATP2A2; ATP2A2; DD; DAR; ATP2B; SERCA2; ATP2B; SERCA2; SR Ca(2+)-ATPase 2

AT2A2_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

314-756, Partial, provide a partial of Cytoplasmic domain.

756

VITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDK
TGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAP
IGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEA
KGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERAN
ACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSM
SKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSV
IREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKY
ETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITG
DNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSA
QRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDG
VNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTI
VAAVEEGRAIYNNM

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cardiovascular

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle.

Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene.Lytton J., Maclennan D.H.J. Biol. Chem. 263:15024-15031(1988) The finished DNA sequence of human chromosome 12.Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) Complete 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) Identification of a new SERCA2 splice variant regulated during monocytic differentiation.Gelebart P., Martin V., Enouf J., Papp B.Biochem. Biophys. Res. Commun. 303:676-684(2003) TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis.Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.Mol. Cell. Biol. 24:1758-1768(2004) Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging.Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.Am. J. Physiol. 290:H2220-H2227(2006) 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) 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) The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival.Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G.Mol. Biol. Cell 20:306-318(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) 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) POST, partner of stromal interaction molecule 1 (STIM1) , targets STIM1 to multiple transporters.Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(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) Spectrum of novel ATP2A2 mutations in patients with Darier's disease.Sakuntabhai A., Burge S., Monk S., Hovnanian A.Hum. Mol. Genet. 8:1611-1619(1999) ATP2A2 mutations in Darier's disease variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class.Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L., Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P., Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G., Munro C.S., Strachan T.Hum. Mol. Genet. 8:1621-1630(1999) ATP2A2 mutations in Darier's disease and their relationship to neuropsychiatric phenotypes.Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y., O'Donovan M.C., Craddock N., Owen M.J.Hum. Mol. Genet. 8:1631-1636(1999) Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease.Sakuntabhai A., Ruiz-Perez V., Carter S., Jacobsen N., Burge S., Monk S., Smith M., Munro C.S., O'Donovan M.C., Craddock N., Kucherlapati R., Rees J.L., Owen M.J., Lathrop G.M., Monaco A.P., Strachan T., Hovnanian A.Nat. Genet. 21:271-277(1999) Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2 evidence that it is allelic to Darier's disease.Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A., MacSween R., Saihan E., Hovnanian A.J. Invest. Dermatol. 120:229-232(2003) Ca2+-ATPases in non-failing and failing heart evidence for a novel cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c) .Dally S., Bredoux R., Corvazier E., Andersen J.P., Clausen J.D., Dode L., Fanchaouy M., Gelebart P., Monceau V., Del Monte F., Gwathmey J.K., Hajjar R., Chaabane C., Bobe R., Raies A., Enouf J.Biochem. J. 395:249-258(2006) Three-base deletion mutation c.120_122delGTT in ATP2A2 leads to the unique phenotype of comedonal Darier disease.Tsuruta D., Akiyama M., Ishida-Yamamoto A., Imanishi H., Mizuno N., Sowa J., Kobayashi H., Ishii M., Kurokawa I., Shimizu H.Br. J. Dermatol. 162:687-689(2010) +Additional computationally mapped references. p>Provides general information on the entry.

4502285

NP_001672.1

NM_001681.3

P16615

52.42kD

Adrenergic Signaling In Cardiomyocytes Pathway (908257); Adrenergic Signaling In Cardiomyocytes Pathway (909696); Alzheimer's Disease Pathway (83097); Alzheimer's Disease Pathway (509); Alzheimers Disease Pathway (672448); Arrhythmogenic Right Ventricular Cardiomyopathy Pathway (672454); Arrhythmogenic Right Ventricular Cardiomyopathy (ARVC) Pathway (117293); Arrhythmogenic Right Ventricular Cardiomyopathy (ARVC) Pathway (116129); Calcium Regulation In The Cardiac Cell Pathway (198906); Calcium Signaling Pathway (83050)

This gene encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the sarcoplasmic reticulum lumen, and is involved in regulation of the contraction/relaxation cycle. Mutations in this gene cause Darier-White disease, also known as keratosis follicularis, an autosomal dominant skin disorder characterized by loss of adhesion between epidermal cells and abnormal keratinization. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2008]

SERCA2: an intracellular pump located in the sarcoplasmic or endoplasmic reticula of muscle cells. Possesses a Ca(2+)-ATPase activity. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in regulation of the contraction/relaxation cycle. Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN. Two alternatively spliced isoforms have been described. Protein type: Transporter; Membrane protein, integral; EC 3.6.3.8; Hydrolase; Endoplasmic reticulum; Membrane protein, multi-pass; Cell adhesion; Transporter, ion channel. Chromosomal Location of Human Ortholog: 12q24.11. Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; extrinsic to internal side of plasma membrane; integral to plasma membrane; membrane; perinuclear region of cytoplasm; protein complex; sarcoplasmic reticulum; sarcoplasmic reticulum membrane; vesicle membrane. Molecular Function: ATP binding; calcium ion binding; calcium-transporting ATPase activity; enzyme binding; lutropin-choriogonadotropic hormone receptor binding; protein binding; protein C-terminus binding. Biological Process: blood coagulation; cell adhesion; cellular calcium ion homeostasis; elevation of endoplasmic reticulum calcium ion concentration; endoplasmic reticulum calcium ion homeostasis; epidermis development; ER-nuclear signaling pathway; metabolic process; negative regulation of heart contraction; organelle organization and biogenesis; positive regulation of heart rate; regulation of the force of heart contraction; response to peptide hormone stimulus; T-tubule organization and biogenesis; transition between fast and slow fiber; transmembrane transport. Disease: Acrokeratosis Verruciformis; Darier-white Disease

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

950

0.05 mg (Mammalian-Cell)

1170