Soluble calcium-activated nucleotidase 1 Recombinant Protein | SHAPY recombinant protein

Recombinant Human Soluble calcium-activated nucleotidase 1

Cat. Num. AAA1265608

• Gene Names: CANT1; DBQD; SCAN1; SHAPY; SCAN-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Soluble calcium-activated nucleotidase 1; Recombinant Human Soluble calcium-activated nucleotidase 1; Apyrase homolog; Putative MAPK-activating protein P; M09; Putative NF-kappa-B-activating protein 107; SHAPY recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 80-397aa; Partial
• Sequence: GQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEG
• Sequence Length: 401

• 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 SHAPY recombinant protein

Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.

Product Categories/Family for SHAPY recombinant protein

Epigenetics and Nuclear Signaling

References

Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases.Smith T., Hicks-Berger C., Kim S., Kirley T.Arch. Biochem. Biophys. 406:105-115(2002) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.Oncogene 22:3307-3318(2003) 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) Cloning, expression, and functional characterization of a Ca2+-dependent endoplasmic reticulum nucleoside diphosphatase.Failer B.U., Braun N., Zimmermann H.J. Biol. Chem. 277:36978-36986(2002) Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1) identification of residues essential for enzyme activity and the Ca(2+) -induced conformational change.Yang M., Kirley T.L.Biochemistry 43:9185-9194(2004) Mutation of CANT1 causes Desbuquois dysplasia.Faden M., Al-Zahrani F., Arafah D., Alkuraya F.S.Am. J. Med. Genet. A 152:1157-1160(2010) Further delineation of CANT1 phenotypic spectrum and demonstration of its role in proteoglycan synthesis.Nizon M., Huber C., De Leonardis F., Merrina R., Forlino A., Fradin M., Tuysuz B., Abu-Libdeh B.Y., Alanay Y., Albrecht B., Al-Gazali L., Basaran S.Y., Clayton-Smith J., Desir J., Gill H., Greally M.T., Koparir E., van Maarle M.C., Mackay S., Mortier G., Morton J., Sillence D., Vilain C., Young I., Zerres K., Le Merrer M., Munnich A., Le Goff C., Rossi A., Cormier-Daire V.Hum. Mutat. 33:1261-1266(2012) Structure and protein design of a human platelet function inhibitor.Dai J., Liu J., Deng Y., Smith T.M., Lu M.Cell 116:649-659(2004) Identification of CANT1 mutations in Desbuquois dysplasia.Huber C., Oules B., Bertoli M., Chami M., Fradin M., Alanay Y., Al-Gazali L.I., Ausems M.G., Bitoun P., Cavalcanti D.P., Krebs A., Le Merrer M., Mortier G., Shafeghati Y., Superti-Furga A., Robertson S.P., Le Goff C., Muda A.O., Paterlini-Brechot P., Munnich A., Cormier-Daire V.Am. J. Hum. Genet. 85:706-710(2009) Desbuquois dysplasia type I and fetal hydrops due to novel mutations in the CANT1 gene.Laccone F., Schoner K., Krabichler B., Kluge B., Schwerdtfeger R., Schulze B., Zschocke J., Rehder H.Eur. J. Hum. Genet. 19:1133-1137(2011) A founder mutation of CANT1 common in Korean and Japanese Desbuquois dysplasia.Dai J., Kim O.H., Cho T.J., Miyake N., Song H.R., Karasugi T., Sakazume S., Ikema M., Matsui Y., Nagai T., Matsumoto N., Ohashi H., Kamatani N., Nishimura G., Furuichi T., Takahashi A., Ikegawa S.J. Hum. Genet. 56:398-400(2011) CANT1 mutation is also responsible for Desbuquois dysplasia, type 2 and Kim variant.Furuichi T., Dai J., Cho T.J., Sakazume S., Ikema M., Matsui Y., Baynam G., Nagai T., Miyake N., Matsumoto N., Ohashi H., Unger S., Superti-Furga A., Kim O.H., Nishimura G., Ikegawa S.J. Med. Genet. 48:32-37(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 229577440
• NCBI GeneID: 124583
• NCBI Accession #: NP_001153244.1
• NCBI GenBank Nucleotide #: NM_001159772.1
• UniProt Accession #: Q8WVQ1; Q7Z2J7; Q8NG05; Q8NHP0; Q9BSD5; B4DJ54
• Molecular Weight: 39.4 kDa
• NCBI Official Full Name: soluble calcium-activated nucleotidase 1
• NCBI Official Synonym Full Names: calcium activated nucleotidase 1
• NCBI Official Symbol: CANT1
• NCBI Official Synonym Symbols: DBQD; SCAN1; SHAPY; SCAN-1
• NCBI Protein Information: soluble calcium-activated nucleotidase 1
• UniProt Protein Name: Soluble calcium-activated nucleotidase 1
• Protein Family: Soluble calcium-activated nucleotidase
• UniProt Gene Name: CANT1
• UniProt Synonym Gene Names: SHAPY; SCAN-1
• UniProt Entry Name: CANT1_HUMAN

NCBI Description

This protein encoded by this gene belongs to the apyrase family. It functions as a calcium-dependent nucleotidase with a preference for UDP. Mutations in this gene are associated with Desbuquois dysplasia with hand anomalies. Alternatively spliced transcript variants have been noted for this gene.[provided by RefSeq, Mar 2010]

Uniprot Description

CANT1: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis. Defects in CANT1 are the cause of Desbuquois dysplasia (DBQD). A chondrodysplasia characterized by severe prenatal and postnatal growth retardation (less than -5 SD), joint laxity, short extremities, progressive scoliosis, round face, midface hypoplasia, prominent bulging eyes. The main radiologic features are short long bones with metaphyseal splay, a 'Swedish key' appearance of the proximal femur (exaggerated trochanter), and advance carpal and tarsal bone age. Two forms of Desbuquois dysplasia are distinguished on the basis of the presence (type 1) or absence (type 2) of characteristic hand anomalies: an extra ossification center distal to the second metacarpal, delta phalanx, bifid distal thumb phalanx, and phalangeal dislocations. Belongs to the apyrase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.6.1.6; Membrane protein, integral; Endoplasmic reticulum; Nucleotide Metabolism - pyrimidine; Hydrolase; Nucleotide Metabolism - purine

Chromosomal Location of Human Ortholog: 17q25.3

Cellular Component: endoplasmic reticulum membrane; integral to membrane

Molecular Function: calcium ion binding; guanosine-diphosphatase activity; signal transducer activity; uridine-diphosphatase activity

Biological Process: positive regulation of I-kappaB kinase/NF-kappaB cascade; proteoglycan biosynthetic process; signal transduction

Disease: Desbuquois Dysplasia 1