protein

Recombinant Human Succinate-semialdehyde dehydrogenase, mitochondrial

MBS955219

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Succinate-semialdehyde dehydrogenase, mitochondrial

Succinate-semialdehyde dehydrogenase

Aldehyde dehydrogenase family 5 member A1; A1NAD(+)-dependent succinic semialdehyde dehydrogenase

succinate-semialdehyde dehydrogenase, mitochondrial isoform 2; Succinate-semialdehyde dehydrogenase, mitochondrial; succinate-semialdehyde dehydrogenase, mitochondrial; aldehyde dehydrogenase 5 family member A1; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase

ALDH5A1

ALDH5A1; ALDH5A1; SSDH; SSADH; SSADH

SSDH_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

48-535

535

AGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAA
LGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLR
KWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFL
EWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITP
WNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAE
LASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKIS
FTGSTTTGKILLHHAANSVKR

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

Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).

Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria) .Chambliss K.L., Hinson D.D., Trettel F., Malaspina P., Novelletto A., Jakobs C., Gibson K.M.Am. J. Hum. Genet. 63:399-408(1998) Structure of human succinic semialdehyde dehydrogenase gene identification of promoter region and alternatively processed isoforms.Blasi P., Boyl P.P., Ledda M., Novelletto A., Gibson K.M., Jakobs C., Hogema B., Akaboshi S., Loreni F., Malaspina P.Mol. Genet. Metab. 76:348-362(2002) 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 analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Molecular cloning of the mature NAD(+) -dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression.Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., Jakobs C., Gibson K.M.J. Biol. Chem. 270:461-467(1995) Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization.Trettel F., Malaspina P., Jodice C., Novelletto A., Slaughter C.A., Caudle D.L., Hinson D.D., Chambliss K.L., Gibson K.M.Adv. Exp. Med. Biol. 414:253-260(1997) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(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) 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) Redox-switch modulation of human SSADH by dynamic catalytic loop.Kim Y.-G., Lee S., Kwon O.-S., Park S.-Y., Lee S.-J., Park B.-J., Kim K.-J.EMBO J. 28:959-968(2009) Prenatal diagnosis of succinic semialdehyde dehydrogenase deficiency increased accuracy employing DNA, enzyme, and metabolite analyses.Hogema B.M., Akaboshi S., Taylor M., Salomons G.S., Jakobs C., Schutgens R.B., Wilcken B., Worthington S., Maropoulos G., Grompe M., Gibson K.M.Mol. Genet. Metab. 72:218-222(2001) Mutation analysis in a patient with succinic semialdehyde dehydrogenase deficiency a compound heterozygote with 103-121del and 1460T>A of the ALDH5A1 gene.Aoshima T., Kajita M., Sekido Y., Ishiguro Y., Tsuge I., Kimura M., Yamaguchi S., Watanabe K., Shimokata K., Niwa T.Hum. Hered. 53:42-44(2002) Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency.Akaboshi S., Hogema B.M., Novelletto A., Malaspina P., Salomons G.S., Maropoulos G.D., Jakobs C., Grompe M., Gibson K.M.Hum. Mutat. 22:442-450(2003)

4507229

NP_001071.1

NM_001080.3

P51649

68.3kD

Alanine, Aspartate And Glutamate Metabolism Pathway (101142); Alanine, Aspartate And Glutamate Metabolism Pathway (100063); Butanoate Metabolism Pathway (83007); Butanoate Metabolism Pathway (391); Degradation Of GABA Pathway (1268777); GABA (gamma-Aminobutyrate) Shunt Pathway (413433); GABA (gamma-Aminobutyrate) Shunt Pathway (468220); GABA Synthesis, Release, Reuptake And Degradation Pathway (1268774); Metabolic Pathways (132956); Neuronal System Pathway (1268763)

This protein belongs to the aldehyde dehydrogenase family of proteins. This gene encodes a mitochondrial NAD(+)-dependent succinic semialdehyde dehydrogenase. A deficiency of this enzyme, known as 4-hydroxybutyricaciduria, is a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA). In response to the defect, physiologic fluids from patients accumulate GHB, a compound with numerous neuromodulatory properties. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]

ALDH5A1: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). Defects in ALDH5A1 are the cause of succinate semialdehyde dehydrogenase deficiency (SSADH deficiency). SSADH deficiency is a rare inborn error in the metabolism of 4-aminobutyric acid (GABA) which leads to accumulation of 4-hydroxybutyric acid in physiologic fluids of patients. The disease is characterized by severe ataxia and by mildly retarded psychomotor development. Belongs to the aldehyde dehydrogenase family. Protein type: Amino Acid Metabolism - alanine, aspartate and glutamate; Mitochondrial; EC 1.2.1.24; Oxidoreductase; Carbohydrate Metabolism - butanoate. Chromosomal Location of Human Ortholog: 6p22. Cellular Component: mitochondrial matrix; mitochondrion. Molecular Function: aldehyde dehydrogenase (NAD) activity; carboxylic acid binding; NAD binding; protein homodimerization activity; succinate-semialdehyde dehydrogenase [NAD(P)+] activity; succinate-semialdehyde dehydrogenase activity. Biological Process: acetate metabolic process; central nervous system development; galactosylceramide metabolic process; gamma-aminobutyric acid catabolic process; glucose metabolic process; glucosylceramide metabolic process; glutamate metabolic process; glutamine metabolic process; glutathione metabolic process; glycerophospholipid metabolic process; neurotransmitter catabolic process; neurotransmitter secretion; post-embryonic development; protein homotetramerization; short-chain fatty acid metabolic process; succinate metabolic process; synaptic transmission. Disease: Succinic Semialdehyde Dehydrogenase Deficiency

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750