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ALDH5A1 recombinant protein :: Succinate-semialdehyde dehydrogenase Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS955219
SDS-PAGE
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
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 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
 Product Gene Name   

ALDH5A1 recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 Sequence Positions    48-535aa; Full Length
 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
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 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.
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 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.
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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    Metabolism
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 SDS-PAGE of ALDH5A1 recombinant protein    ALDH5A1 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for ALDH5A1. It may not necessarily be applicable to this product.
 NCBI GI #    4507229
 NCBI GeneID    7915
 NCBI Accession #    NP_001071.1 [Other Products]
 NCBI GenBank Nucleotide #    NM_001080.3 [Other Products]
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 UniProt Primary Accession #    P51649 [Other Products]
 UniProt Secondary Accession #    Q546H9; Q8N3W6; B2RD26; G5E949 [Other Products]
 UniProt Related Accession #    P51649 [Other Products]
 Molecular Weight    68.3kD
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 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
 Protein Family    Succinate-semialdehyde dehydrogenase
 UniProt Gene Name    ALDH5A1 [Similar Products]
 UniProt Synonym Gene Names    SSADH [Similar Products]
 UniProt Entry Name    SSDH_HUMAN
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 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]
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 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
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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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 Research Articles on ALDH5A1    1. Pearl et al. identify 3 new pathogenic mutations in the ALDH5A1 gene previously unreported in the literature. EXON: 1 Nucleotide change: c.412 C>T Change in protein: p.L138F EXON: 4 Nucleotide change: c.754G>T Change in protein: p.Q252X EXON: 8 Nucleotide change: c.1360G>A Change in protein: p.A454T
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 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.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Products associated with ALDH5A1 recombinant proteinPathways associated with ALDH5A1 recombinant protein
 Reference Product  PubMed Publications
 ABAT recombinant protein  >1 publications with ALDH5A1 and ABAT
 Products by Pathway  Pathway Diagram
 Alanine, Aspartate And Glutamate Metabolism Pathway antibodies  Alanine, Aspartate And Glutamate Metabolism Pathway Diagram
 Alanine, Aspartate And Glutamate Metabolism Pathway antibodies  Alanine, Aspartate And Glutamate Metabolism Pathway Diagram
 Butanoate Metabolism Pathway antibodies  Butanoate Metabolism Pathway Diagram
 Butanoate Metabolism Pathway antibodies  Butanoate Metabolism Pathway Diagram
 Degradation Of GABA Pathway antibodies  Degradation Of GABA Pathway Diagram
 GABA (gamma-Aminobutyrate) Shunt Pathway antibodies  GABA (gamma-Aminobutyrate) Shunt Pathway Diagram
 GABA (gamma-Aminobutyrate) Shunt Pathway antibodies  GABA (gamma-Aminobutyrate) Shunt Pathway Diagram
 GABA Synthesis, Release, Reuptake And Degradation Pathway antibodies  GABA Synthesis, Release, Reuptake And Degradation Pathway Diagram
 Metabolic Pathways antibodies  Metabolic Pathways Diagram
 Neuronal System Pathway antibodies  Neuronal System Pathway Diagram
Diseases associated with ALDH5A1 recombinant proteinOrgans/Tissues associated with ALDH5A1 recombinant protein
 Disease Name  Pubmed Publications
 succinic semialdehyde dehydrogenase deficiency Antibodies  >52 publications with ALDH5A1 and succinic semialdehyde dehydrogenase deficiency
 Nervous System Diseases Antibodies  >39 publications with ALDH5A1 and Nervous System Diseases
 Neurobehavioral Manifestations Antibodies  >16 publications with ALDH5A1 and Neurobehavioral Manifestations
 Disease Models, Animal Antibodies  >9 publications with ALDH5A1 and Disease Models, Animal
 Intellectual Disability Antibodies  >9 publications with ALDH5A1 and Intellectual Disability
 Brain Diseases, Metabolic Antibodies  >6 publications with ALDH5A1 and Brain Diseases, Metabolic
 Poisoning Antibodies  >3 publications with ALDH5A1 and Poisoning
 Liver Diseases Antibodies  >2 publications with ALDH5A1 and Liver Diseases
 Neurotoxicity Syndromes Antibodies  >2 publications with ALDH5A1 and Neurotoxicity Syndromes
 Liver Neoplasms Antibodies  >1 publications with ALDH5A1 and Liver Neoplasms
 Organ/Tissue Name  Pubmed Publications
 Brain Antibodies  >60 publications with ALDH5A1 and Brain
 Liver Antibodies  >14 publications with ALDH5A1 and Liver
 Muscle Antibodies  >8 publications with ALDH5A1 and Muscle
 Kidney Antibodies  >6 publications with ALDH5A1 and Kidney
 Embryonic Tissue Antibodies  >4 publications with ALDH5A1 and Embryonic Tissue
 Eye Antibodies  >3 publications with ALDH5A1 and Eye
 Heart Antibodies  >2 publications with ALDH5A1 and Heart
 Intestine Antibodies  >1 publications with ALDH5A1 and Intestine
 Ovary Antibodies  >1 publications with ALDH5A1 and Ovary
 Pancreas Antibodies  >1 publications with ALDH5A1 and Pancreas
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