protein

Recombinant Human Ganglioside GM2 activator protein

MBS717112

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Ganglioside GM2 activator protein

Ganglioside GM2 activator protein

Cerebroside sulfate activator protein; GM2-AP; Sphingolipid activator protein 3; SAP-3

ganglioside GM2 activator isoform 1; Ganglioside GM2 activator; ganglioside GM2 activator; GM2 ganglioside activator; Cerebroside sulfate activator protein; GM2-AP; Sphingolipid activator protein 3; SAP-3

GM2A

GM2A; GM2A; SAP-3; GM2-AP; SAP-3

SAP3_HUMAN

E Coli

32-193

193

SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMG
STSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFE
HFCDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLP
KSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIA
ASLKGI

Greater than 90% as determined by SDS-PAGE.

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

Metabolism

The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents th in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.

Isolation and expression of a full-length cDNA encoding the human G-M2 activator protein.Xie B., McInnes B., Neote K., Lamhonwah A.-M., Mahuran D.Biochem. Biophys. Res. Commun. 177:1217-1223(1991) Characterization of full-length cDNAs and the gene coding for the human GM2 activator protein.Klima H., Tanaka A., Schnabel D., Nakano T., Schroeder M., Suzuki K., Sandhoff K.FEBS Lett. 289:260-264(1991) Evidence for two cDNAs encoding human GM2-activator protein.Nagarajan S., Chen H.C., Li S.C., Li Y.T., Lockyer J.Biochem. J. 282:807-813(1992) Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5.Xie B., Kennedy J.L., McInnes B., Auger D., Mahuran D.J.Genomics 14:796-798(1992) 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 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004) Structure of the GM2A gene identification of an exon 2 nonsense mutation and a naturally occurring transcript with an in-frame deletion of exon 2.Chen B., Rigat B., Curry C., Mahuran D.J.Am. J. Hum. Genet. 65:77-87(1999)

39995109

NP_000396.2

NM_000405.4

P17900

45kD

Glycosphingolipid Metabolism Pathway (1270099); Lysosome Pathway (99052); Lysosome Pathway (96865); Metabolism Pathway (1269956); Metabolism Of Lipids And Lipoproteins Pathway (1270001); Sphingolipid Metabolism Pathway (1270097)

This gene encodes a small glycolipid transport protein which acts as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. Beta-hexosaminidase A, together with GM2 ganglioside activator, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Mutations in this gene result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2009]

GM2A: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta- hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. Defects in GM2A are the cause of GM2-gangliosidosis type AB (GM2GAB); also known as Tay-Sachs disease AB variant. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2GAB is characterized by GM2 gangliosides accumulation in the presence of both hexosaminidase A and B. Protein type: Activator; Mitochondrial. Chromosomal Location of Human Ortholog: 5q33.1. Cellular Component: apical cortex; hydrogen:potassium-exchanging ATPase complex; internal side of plasma membrane; lysosomal lumen; mitochondrion. Molecular Function: beta-N-acetylgalactosaminidase activity; lipid transporter activity; phospholipase activator activity. Biological Process: ganglioside catabolic process; glycosphingolipid metabolic process; learning and/or memory; lipid transport; neuromuscular process controlling balance; oligosaccharide catabolic process; positive regulation of hydrolase activity; sequestering of lipid; sphingolipid metabolic process. Disease: Gm2-gangliosidosis, Ab Variant

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180