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ALDH5A1 recombinant protein :: Succinate-semialdehyde dehydrogenase Recombinant Protein

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Catalog # MBS955219
Unit / Price
  0.01 mg (Yeast)  /  $110 +1 FREE 8GB USB
  0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $190 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
  0.1 mg (Yeast)  /  $285 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $460 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $750 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $1,115 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,180 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,365 +1 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,420 +1 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $2,035 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $2,065 +2 FREE 8GB USB
  1 mg (Baculovirus)  /  $2,675 +3 FREE 8GB USB
SDS-PAGE
Product Name

Succinate-semialdehyde dehydrogenase (ALDH5A1), Recombinant Protein

Popular Item
Also Known As

Recombinant Human Succinate-semialdehyde dehydrogenase, mitochondrial

Product Synonym Names
Aldehyde dehydrogenase family 5 member A1; A1NAD(+)-dependent succinic semialdehyde dehydrogenase
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
48-535aa; Full Length
Sequence Length
535
Sequence
AGRLAGLSAA LLRTDSFVGG RWLPAAATFP VQDPASGAAL GMVADCGVRE ARAAVRAAYE AFCRWREVSA KERSSLLRKW YNLMIQNKDD LARIITAESG KPLKEAHGEI LYSAFFLEWF SEEARRVYGD IIHTPAKDRR ALVLKQPIGV AAVITPWNFP SAMITRKVGA ALAAGCTVVV KPAEDTPFSA LALAELASQA GIPSGVYNVI PCSRKNAKEV GEAICTDPLV SKISFTGSTT TGKILLHHAA NSVKRVSMEL GGLAPFIVFD SANVDQAVAG AMASKFRNTG QTCVCSNQFL VQRGIHDAFV KAFAEAMKKN LRVGNGFEEG TTQGPLINEK AVEKVEKQVN DAVSKGATVV TGGKRHQLGK NFFEPTLLCN VTQDMLCTHE ETFGPLAPVI KFDTEEEAIA IANAADVGLA GYFYSQDPAQ IWRVAEQLEV GMVGVNEGLI SSVECPFGGV KQSGLGREGS KYGIDEYLEL KYVCYGGL
OMIM
271980
3D Structure
ModBase 3D Structure for P51649
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of ALDH5A1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
ALDH5A1 recombinant protein
Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
Product Categories/Family for ALDH5A1 recombinant protein

ALDH5A1 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for ALDH5A1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
68.3kD
NCBI Official Full Name
succinate-semialdehyde dehydrogenase, mitochondrial isoform 2
NCBI Official Synonym Full Names
aldehyde dehydrogenase 5 family member A1
NCBI Official Symbol
ALDH5A1  [Similar Products]
NCBI Official Synonym Symbols
SSDH; SSADH
  [Similar Products]
NCBI Protein Information
succinate-semialdehyde dehydrogenase, mitochondrial
UniProt Protein Name
Succinate-semialdehyde dehydrogenase, mitochondrial
UniProt Synonym Protein Names
Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase
UniProt Gene Name
ALDH5A1  [Similar Products]
UniProt Synonym Gene Names
SSADH  [Similar Products]
UniProt Entry Name
SSDH_HUMAN
NCBI Summary for ALDH5A1
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]
UniProt Comments for ALDH5A1
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
Product References and Citations for ALDH5A1 recombinant protein
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)

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Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

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