Phospholysine phosphohistidine inorganic pyrophosphate phosphatase  Recombinant Protein | LHPP recombinant protein

Recombinant Human Phospholysine phosphohistidine inorganic pyrophosphate phosphatase 

Cat. Num. AAA1478066

• Gene Names: LHPP; HDHD2B
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Phospholysine phosphohistidine inorganic pyrophosphate phosphatase ; Recombinant Human Phospholysine phosphohistidine inorganic pyrophosphate phosphatase ; LHPP 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: 1-270aa; Full Length
• Sequence: MAPWGKRLAGVRGVLLDISGVLYDSGAGGGTAIAGSVEAVARLKRSRLKVRFCTNESQKSRAELVGQLQRLGFDISEQEVTAPAPAACQILKEQGLRPYLLIHDGVRSEFDQIDTSNPNCVVIADAGESFSYQNMNNAFQVLMELEKPVLISLGKGRYYKETSGLMLDVGPYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQAVMIGDDIVGDVGGAQRCGMRALQVRTGKFRPSDEHHPEVKADGYVDNLAEAVDLLLQHADK
• Sequence Length: 210

• 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 LHPP recombinant protein

Phosphatase that hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency.

Product Categories/Family for LHPP recombinant protein

Metabolism

References

Molecular cloning of a cDNA for the human phospholysine phosphohistidine inorganic pyrophosphate phosphatase.Yokoi F., Hiraishi H., Izuhara K.J. Biochem. 133:607-614(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) 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) Expression of new human inorganic pyrophosphatase in thyroid diseases its intimate association with hyperthyroidism.Koike E., Toda S., Yokoi F., Izuhara K., Koike N., Itoh K., Miyazaki K., Sugihara H.Biochem. Biophys. Res. Commun. 341:691-696(2006) 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) Crystal structure of human phospholysine phosphohistidine inorganic pyrophosphate phosphatase LHPP.Structural genomics consortium (SGC) Submitted (MAR-2010) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 269847104
• NCBI GeneID: 64077
• NCBI Accession #: NP_001161352.1
• NCBI GenBank Nucleotide #: NM_001167880.1
• UniProt Accession #: Q9H008; Q2TBE9; Q5VUV9; Q5VUW0; B3KP20
• Molecular Weight: 31.2 kDa
• NCBI Official Full Name: phospholysine phosphohistidine inorganic pyrophosphate phosphatase isoform 2
• NCBI Official Synonym Full Names: phospholysine phosphohistidine inorganic pyrophosphate phosphatase
• NCBI Official Symbol: LHPP
• NCBI Official Synonym Symbols: HDHD2B
• NCBI Protein Information: phospholysine phosphohistidine inorganic pyrophosphate phosphatase
• UniProt Protein Name: Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
• Protein Family: Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
• UniProt Gene Name: LHPP
• UniProt Synonym Gene Names: hLHPP
• UniProt Entry Name: LHPP_HUMAN

Uniprot Description

LHPP: Phosphatase that hydrolyzes imidodiphosphate, 3- phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency. Belongs to the HAD-like hydrolase superfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Mitochondrial; EC 3.6.1.1; Hydrolase; Energy Metabolism - oxidative phosphorylation

Chromosomal Location of Human Ortholog: 10q26.13

Cellular Component: cytoplasm; cytosol; nucleoplasm; nucleus

Molecular Function: inorganic diphosphatase activity; magnesium ion binding; phosphohistidine phosphatase activity; protein homodimerization activity

Biological Process: nucleobase, nucleoside and nucleotide metabolic process; phosphate metabolic process; protein amino acid dephosphorylation; purine base metabolic process; purine ribonucleoside monophosphate biosynthetic process