protein

Recombinant Human Indolethylamine N-methyltransferase

MBS1011652

0.05 mg (E-Coli)

180 USD

Recombinant Protein

Recombinant Human Indolethylamine N-methyltransferase

Indolethylamine N-methyltransferase

Aromatic alkylamine N-methyltransferase; Amine N-methyltransferase; Arylamine N-methyltransferaseThioether S-methyltransferase; TEMT

indolethylamine N-methyltransferase isoform 2; Indolethylamine N-methyltransferase; indolethylamine N-methyltransferase; indolethylamine N-methyltransferase; Aromatic alkylamine N-methyltransferase; Amine N-methyltransferase; Arylamine N-methyltransferase; Thioether S-methyltransferase; TEMT

INMT

INMT; INMT; TEMT; Indolamine N-methyltransferase; Amine N-methyltransferase; Arylamine N-methyltransferase; TEMT

INMT_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-263, Full length.

263

MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLK
FNLECLHKTFGPGGLQGDTLIDIGSGPTIYQVLAACDSF
QDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACEL
EGNSGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPL
ADCVLTLLAMECACCSLDAYRAALCNLASLLKPGGHLVT
TVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQ
LLHSPQSYSVTNAANNGVCFIVARKKPGP

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.

Metabolism

Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds. Catalyzes the N-methylation of tryptamine and structurally related compounds. 1 Publication

Human indolethylamine N-methyltransferase cDNA cloning and expression, gene cloning, and chromosomal localization.Thompson M.A., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M.Genomics 61:285-297(1999) 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 of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003) Human-specific amino acid changes found in 103 protein-coding genes.Kitano T., Liu Y.-H., Ueda S., Saitou N.Mol. Biol. Evol. 21:936-944(2004) The crystal structure of human indolethylamine N-methyltransferase in complex with SAH.Structural genomics consortium (SGC) Submitted (JUN-2005) to the PDB data bank

312836856

NP_001186148.1

NM_001199219.1

O95050

44.8kD

Metabolism Pathway (1269956); Metabolism Of Amino Acids And Derivatives Pathway (1270158); Methylation Of MeSeH For Excretion Pathway (1339152); Selenoamino Acid Metabolism Pathway (1339149); Selenocompound Metabolism Pathway (82969); Selenocompound Metabolism Pathway (338); Tryptophan Metabolism Pathway (82964); Tryptophan Metabolism Pathway (198850); Tryptophan Metabolism Pathway (332); Nicotine Degradation IV Pathway (142437)

N-methylation of endogenous and xenobiotic compounds is a major method by which they are degraded. This gene encodes an enzyme that N-methylates indoles such as tryptamine. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the downstream FAM188B (family with sequence similarity 188, member B) gene. [provided by RefSeq, Nov 2010]

INMT: Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2- methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds. Catalyzes the N-methylation of tryptamine and structurally related compounds. Belongs to the NNMT/PNMT/TEMT family. Protein type: EC 2.1.1.96; Methyltransferase; EC 2.1.1.49; Amino Acid Metabolism - tryptophan. Chromosomal Location of Human Ortholog: 7p14.3. Cellular Component: cytosol. Molecular Function: amine N-methyltransferase activity; protein binding; thioether S-methyltransferase activity. Biological Process: amine metabolic process; methylation; response to toxin; selenium metabolic process

0.05 mg (E-Coli)

180 USD

0.2 mg (E-Coli)

490

0.5 mg (E-Coli)

715

0.05 mg (Baculovirus)

950

1 mg (E-Coli)

1170