Multiple inositol polyphosphate phosphatase 1 Recombinant Protein | MINPP1 recombinant protein

Recombinant Human Multiple inositol polyphosphate phosphatase 1

Cat. Num. AAA1451758

• Gene Names: MINPP1; MIPP; HIPER1; MINPP2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Multiple inositol polyphosphate phosphatase 1; Recombinant Human Multiple inositol polyphosphate phosphatase 1; 2; 3-bisphosphoglycerate 3-phosphatase (EC:3.1.3.80); 3-BPG phosphataseInositol (1; 3; 4; 5)-tetrakisphosphate 3-phosphatase; Ins(1; 5)P(4) 3-phosphatase; MINPP1 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: 31-487aa; Full Length of Mature Protein
• Sequence: SLLEPRDPVASSLSPYFGTKTRYEDVNPVLLSGPEAPWRDPELLEGTCTPVQLVALIRHGTRYPTVKQIRKLRQLHGLLQARGSRDGGASSTGSRDLGAALADWPLWYADWMDGQLVEKGRQDMRQLALRLASLFPALFSRENYGRLRLITSSKHRCMDSSAAFLQGLWQHYHPGLPPPDVADMEFGPPTVNDKLMRFFDHCEKFLTEVEKNATALYHVEAFKTGPEMQNILKKVAATLQVPVNDLNADLIQVAFFTCSFDLAIKGVKSPWCDVFDIDDAKVLEYLNDLKQYWKRGYGYTINSRSSCTLFQDIFQHLDKAVEQKQRSQPISSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNYKKQMHRKFRSGLIVPYASNLIFVLYHCENAKTPKEQFRVQMLLNEKVLPLAYSQETVSFYEDLKNHYKDILQSCQTSEECELARANSTSDEL
• Sequence Length: 312

• Production Note: Special Offer: The Yeast host-expressed protein is manufactured from a stock plasmid containing the protein gene. Yeasthost-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 Yeast 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 Yeast 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 MINPP1 recombinant protein

Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification).

Product Categories/Family for MINPP1 recombinant protein

Signal Transduction

References

The human and rat forms of multiple inositol polyphosphate phosphatase functional homology with a histidine acid phosphatase up-regulated during endochondral ossification.Caffrey J.J., Hidaka K., Matsuda M., Hirata M., Shears S.B.FEBS Lett. 442:99-104(1999) Multiple inositol polyphosphate phosphatase evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19.Chi H., Tiller G.E., Dasouki M.J., Romano P.R., Wang J., O'keefe R.J., Puzas J.E., Rosier R.N., Reynolds P.R.Genomics 56:324-336(1999) Towards a catalog of human genes and proteins sequencing and analysis of 500 novel complete protein coding human cDNAs.Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.Genome Res. 11:422-435(2001) The secreted protein discovery initiative (SPDI) , a large-scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment.Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.Genome Res. 13:2265-2270(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) Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. The DNA sequence and comparative analysis of human chromosome 10.Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.Nature 429:375-381(2004) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt.Cho J., King J.S., Qian X., Harwood A.J., Shears S.B.Proc. Natl. Acad. Sci. U.S.A. 105:5998-6003(2008) 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) Somatic mutation and germline variants of MINPP1, a phosphatase gene located in proximity to PTEN on 10q23.3, in follicular thyroid carcinomas.Gimm O., Chi H., Dahia P.L., Perren A., Hinze R., Komminoth P., Dralle H., Reynolds P.R., Eng C.J. Clin. Endocrinol. Metab. 86:1801-1805(2001)

NCBI and Uniprot Product Information

• NCBI GI #: 296010986
• NCBI GeneID: 9562
• NCBI Accession #: NP_001171588.1
• NCBI GenBank Nucleotide #: NM_001178117.1
• UniProt Accession #: Q9UNW1; O95172; O95286; Q59EJ2; Q9UGA3; F5H683
• Molecular Weight: 54.1 kDa
• NCBI Official Full Name: multiple inositol polyphosphate phosphatase 1 isoform 2
• NCBI Official Synonym Full Names: multiple inositol-polyphosphate phosphatase 1
• NCBI Official Symbol: MINPP1
• NCBI Official Synonym Symbols: MIPP; HIPER1; MINPP2
• NCBI Protein Information: multiple inositol polyphosphate phosphatase 1
• UniProt Protein Name: Multiple inositol polyphosphate phosphatase 1
• Protein Family: Multiple inositol polyphosphate phosphatase
• UniProt Gene Name: MINPP1
• UniProt Synonym Gene Names: MIPP; 2,3-BPG phosphatase; Ins(1,3,4,5)P(4) 3-phosphatase
• UniProt Entry Name: MINP1_HUMAN

NCBI Description

This gene encodes multiple inositol polyphosphate phosphatase; an enzyme that removes 3-phosphate from inositol phosphate substrates. It is the only enzyme known to hydrolzye inositol pentakisphosphate and inositol hexakisphosphate. This enzyme also converts 2,3 bisphosphoglycerate (2,3-BPG) to 2-phosphoglycerate; an activity formerly thought to be exclusive to 2,3-BPG synthase/2-phosphatase (BPGM) in the Rapoport-Luebering shunt of the glycolytic pathway.[provided by RefSeq, Sep 2009]

Uniprot Description

MINPP1: Acts as a phosphoinositide 5- and phosphoinositide 6- phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3- phosphoglycerate. May play a role in bone development (endochondral ossification). Defects in MINPP1 may be involved in follicular thyroid tumors development. Belongs to the histidine acid phosphatase family. MINPP1 subfamily. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.1.3.62; Carbohydrate Metabolism - inositol phosphate; Secreted; Hydrolase; Motility/polarity/chemotaxis; Secreted, signal peptide; EC 3.1.3.80

Chromosomal Location of Human Ortholog: 10q23

Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen

Molecular Function: acid phosphatase activity; phosphohistidine phosphatase activity

Biological Process: bone mineralization; dephosphorylation; inositol phosphate metabolic process; ossification; polyphosphate metabolic process

Disease: Thyroid Carcinoma, Follicular