Recombinant Human Succinate-Semialdehyde Dehydrogenase, Mitochondrial (ALDH5A1) Protein (His-SUMO)

Name: Recombinant Human Succinate-Semialdehyde Dehydrogenase, Mitochondrial (ALDH5A1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10809P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Succinate-Semialdehyde Dehydrogenase, Mitochondrial (ALDH5A1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P51649
Target Symbol	ALDH5A1
Synonyms	Aldedehyde dehydrogenase 5 family; Aldehyde dehydrogenase 5 family member A1; Aldehyde dehydrogenase 5A1; Aldehyde dehydrogenase family 5 member A1; ALDH5A 1; Aldh5a1; mitochondrial; Mitochondrial succinate semialdehyde dehydrogenase; NAD(+) dependent succinic semialdehyde dehydrogenase; NAD(+)-dependent succinic semialdehyde dehydrogenase; SSADH; SSDH; SSDH_HUMAN; Succinate semialdehyde dehydrogenase; Succinate-semialdehyde dehydrogenase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
Expression Range	48-535aa
Protein Length	Full Length of Mature Protein
Mol. Weight	68.3kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
Subcellular Location	Mitochondrion.
Protein Families	Aldehyde dehydrogenase family
Database References	HGNC: 408 OMIM: 271980 KEGG: hsa:7915 STRING: 9606.ENSP00000314649 UniGene: Hs.371723
Associated Diseases	Succinic semialdehyde dehydrogenase deficiency (SSADHD)
Tissue Specificity	Brain, pancreas, heart, liver, skeletal muscle and kidney. Lower in placenta.

Gene Functions References

By ALDH5A1 gene expression in transiently transfected HEK293 cells and enzyme activity assays, we demonstrate that the p.V500 L mutation, despite being conservative, produces complete loss of enzyme activity PMID: 28664505
ALDH5A1 mRNA expression was down-regulated in ovarian cancer patients compared with that in normal tissues. PMID: 28346042
SSADH catalytic loop role in the SSADH redox-switch modulation PMID: 26422261
The proband was found to have compound heterozygous mutations of the succinate-semialdehyde dehydrogenase (ALDH5A1) gene, namely c.398_399delAA (p.N134X) and c.638G>T (p.R213L), for which her parents were both heterozygous carriers. PMID: 28186584
Two novel ALDH5A1 mutations likely responsible for SSADH deficiency were identified, and DNA sequencing provided an accurate diagnosis for an at-risk fetus whose sibling had SSADH deficiency. Current study and literature review identified nine additional novel mutations in eight unrelated families bringing the number of unique mutations of ALDH5A1 resulting in SSADH deficiency to 44, occurring from exon 1 to exon 10. PMID: 25431891
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 PMID: 25558043
Missense mutation in ALDH5A1 is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability. PMID: 23825041
Results show that opioid-dependent patients carrying the T allele of a functional variant in ALDH5A1 had a greater risk of being nonresponders to methadone maintenance treatment PMID: 24230997
The strongest association signal arose from an intronic region of the gene ALDH5A1, which encodes the mitochondrial enzyme succinic semialdehyde dehydrogenase (SSADH), an enzyme involved in gamma-aminobutyric acid metabolism. PMID: 24327614
Missense mutations of c.527G>A and c.691G>A in the ALDH5A1 gene are associated with pathogenesis of succinic semialdehyde dehydrogenase deficiency. PMID: 23926001
Succinic semialdehyde dehydrognase deficiency is caused by a mutation of the Aldh5a1-gene resulting in a dysfunction of the enzyme succinic semialdehyde dehydrogenase--{REVIEW} PMID: 23516105
our study identified a novel homozygous ALDH5A1 gene mutation associated with SSADH deficiency. PMID: 22437753
Study seeks to determine whether cerebellar abnormalities are present in human succinic semialdehyde dehydrogenase deficiency on volumetric MRI, compared with radiographic and histologic studies in the mouse model. PMID: 20445195
the duplication (6)(p22.2) and corresponding hyperactive level of SSADH activity may have negative consequences for GABA metabolism PMID: 21438145
This study indicated that global disruption of cortical networks in SSADH KO mice, affecting both excitatory and inhibitory neurons. PMID: 20363598
High activity of this protein probably indicates disorders in lymphocyte energy state. PMID: 12629812
Higher SSADH activity is associated with higher intelligence across the general population. PMID: 14981524
The unexpected pattern of human SSADH polymorphism compared to interspecific findings outlines the possibility of a recent positive selection on some variants relevant to new cognitive capabilities unique to humans. PMID: 16786440
Deficiency in humans causes ggamma-hydroxybutyric aciduria. PMID: 17457693
within the 65-85 years age range, the T/T genotype is overrepresented in subjects with impaired cognitive function PMID: 18505418
Redox-switch modulation of human SSADH by dynamic catalytic loop PMID: 19300440
SSADH deficient patients have widespread reduction in benzodiazepine receptor (BZPR) binding, suggested by high endogenous brain GABA levels that downregulate GABA(A)-BZPR binding site availability. PMID: 19667317

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.