5-formyltetrahydrofolate cyclo-ligase Recombinant Protein | MTHFS recombinant protein

Recombinant Human 5-formyltetrahydrofolate cyclo-ligase

Cat. Num. AAA953772

• Gene Names: MTHFS; HsT19268
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: 5-formyltetrahydrofolate cyclo-ligase; Recombinant Human 5-formyltetrahydrofolate cyclo-ligase; 5; 10-methenyl-tetrahydrofolate synthetase; MTHFS; Methenyl-THF synthetase; MTHFS 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: 2-203aa; Full Length of Mature Protein
• Sequence: AAAAVSSAKRSLRGELKQRLRAMSAEERLRQSRVLSQKVIAHSEYQKSKRISIFLSMQDEIETEEIIKDIFQRGKICFIPRYRFQSNHMDMVRIESPEEISLLPKTSWNIPQPGEGDVREEALSTGGLDLIFMPGLGFDKHGNRLGRGKGYYDAYLKRCLQHQEVKPYTLALAFKEQICLQVPVNENDMKVDEVLYEDSSTA

• 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 MTHFS recombinant protein

Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-methenyltetrahydrofolate.

Product Categories/Family for MTHFS recombinant protein

Metabolism

References

Cloning and characterization of the human 5,10-methenyltetrahydrofolate synthetase-encoding cDNA.Dayan A., Bertrand R., Beauchemin M., Chahla D., Mamo A., Filion M., Skup D., Massie B., Jolivet J.Gene 165:307-311(1995) Analysis of the DNA sequence and duplication history of human chromosome 15.Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.Nature 440:671-675(2006) Human liver methenyltetrahydrofolate synthetase improved purification and increased affinity for folate polyglutamate substrates.Bertrand R., MacKenzie R.E., Jolivet J.Biochim. Biophys. Acta 911:154-161(1987) 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) 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) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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) Structural basis for the inhibition of human 5,10-methenyltetrahydrofolate synthetase by N10-substituted folate analogues.Wu D., Li Y., Song G., Cheng C., Zhang R., Joachimiak A., Shaw N., Liu Z.-J.Cancer Res. 69:7294-7301(2009)

NCBI and Uniprot Product Information

• NCBI GI #: 315113868
• NCBI GeneID: 10588
• NCBI Accession #: NP_001186687.1
• NCBI GenBank Nucleotide #: NM_001199758.1
• UniProt Accession #: P49914; H3BQ75
• Molecular Weight: 39.1 kDa
• NCBI Official Full Name: 5-formyltetrahydrofolate cyclo-ligase isoform b
• NCBI Official Synonym Full Names: 5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase)
• NCBI Official Symbol: MTHFS
• NCBI Official Synonym Symbols: HsT19268
• NCBI Protein Information: 5-formyltetrahydrofolate cyclo-ligase
• UniProt Protein Name: 5-formyltetrahydrofolate cyclo-ligase
• Protein Family: 5-formyltetrahydrofolate cyclo-ligase
• UniProt Gene Name: MTHFS
• UniProt Synonym Gene Names: MTHFS; Methenyl-THF synthetase
• UniProt Entry Name: MTHFS_HUMAN

NCBI Description

The protein encoded by this gene is an enzyme that catalyzes the conversion of 5-formyltetrahydrofolate to 5,10-methenyltetrahydrofolate, a precursor of reduced folates involved in 1-carbon metabolism. An increased activity of the encoded protein can result in an increased folate turnover rate and folate depletion. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Jun 2011]

Uniprot Description

Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-methenyltetrahydrofolate.