Recombinant Human Very long-chain acyl-CoA synthetase | MyBioSource MBS1032322 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Very long-chain acyl-CoA synthetase

catalog :

MBS1032322

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS1032322

products type :

Recombinant Protein

products full name :

Recombinant Human Very long-chain acyl-CoA synthetase

products short name :

Very long-chain acyl-CoA synthetase

products name syn :

Fatty acid transport protein 2; FATP-2; Fatty-acid-coenzyme A ligase, very long-chain 1; Long-chain-fatty-acid-CoA ligase (EC:6.2.1.3); Solute carrier family 27 member 2; THCA-CoA ligase; Very long-chain-fatty-acid-CoA ligase

other names :

very long-chain acyl-CoA synthetase isoform 2; Very long-chain acyl-CoA synthetase; very long-chain acyl-CoA synthetase; solute carrier family 27 (fatty acid transporter), member 2; Fatty acid transport protein 2; FATP-2; Fatty-acid-coenzyme A ligase, very long-chain 1; Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3); Solute carrier family 27 member 2; THCA-CoA ligase; Very long-chain-fatty-acid-CoA ligase

products gene name :

SLC27A2

other gene names :

SLC27A2; SLC27A2; VLCS; FATP2; VLACS; ACSVL1; FACVL1; hFACVL1; HsT17226; ACSVL1; FACVL1; FATP2; VLACS; VLACS; VLCS; FATP-2

uniprot entry name :

S27A2_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

283-620

sequence length :

567

sequence :

GATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCN
SPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYE
FYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKY
DVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGY
AGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYF
HDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVH
VPDHEGRIGMASIKMKENHEF

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Metabolism

products description :

Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes.

products references :

Molecular cloning of a possible human homolog of the rat very-long-chain acyl-CoA synthetase cDNA and its chromosomal localization.Uchiyama A., Aoyama T., Kamijo K., Wakui K., Fukushima Y., Shimozawa N., Suzuki Y., Kondo N., Orii T., Hashimoto T. Human very-long-chain acyl-CoA synthetase cloning, topography, and relevance to branched-chain fatty acid metabolism.Steinberg S.J., Wang S.J., Kim D.G., Mihalik S.J., Watkins P.A.Biochem. Biophys. Res. Commun. 257:615-621(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) Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. 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)

ncbi gi num :

227499621

ncbi acc num :

NP_001153101.1

ncbi gb acc num :

NM_001159629.1

uniprot acc num :

O14975

ncbi mol weight :

54.8kD

ncbi pathways :

Alpha-oxidation Of Phytanate Pathway (1270032); Bile Acid And Bile Salt Metabolism Pathway (1270040); Insulin Resistance Pathway (1272486); Metabolism Pathway (1269956); Metabolism Of Lipids And Lipoproteins Pathway (1270001); PPAR Signaling Pathway (83042); PPAR Signaling Pathway (450); Peroxisomal Lipid Metabolism Pathway (1270031); Peroxisome Pathway (131226); Peroxisome Pathway (131126)

ncbi summary :

The protein encoded by this gene is an isozyme of long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme activates long-chain, branched-chain and very-long-chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes, but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2009]

uniprot summary :

SLC27A2: Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes. Belongs to the ATP-dependent AMP-binding enzyme family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: EC 6.2.1.3; Ligase; Membrane protein, multi-pass; Membrane protein, integral. Chromosomal Location of Human Ortholog: 15q21.2. Cellular Component: endoplasmic reticulum lumen; endoplasmic reticulum membrane; integral to endoplasmic reticulum membrane; integral to peroxisomal membrane; mitochondrion; peroxisomal membrane. Molecular Function: ATP binding; enzyme binding; fatty acid transporter activity; long-chain-fatty-acid-CoA ligase activity; phytanate-CoA ligase activity; receptor binding; very-long-chain-fatty-acid-CoA ligase activity. Biological Process: bile acid biosynthetic process; bile acid metabolic process; cellular lipid metabolic process; fatty acid alpha-oxidation; fatty acid beta-oxidation; long-chain fatty acid metabolic process; very-long-chain fatty acid catabolic process

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.05 mg (Yeast)

price2 :

190

size3 :

0.2 mg (E-Coli)

price3 :

460

size4 :

0.2 mg (Yeast)

price4 :

460

size5 :

0.5 mg (E-Coli)

price5 :

750

more info or order :

MyBioSource product webpage