Analytical Data
-
Gene name
SUCLA2
- Application
-
Alternative Names
(ATP-specific succinyl-CoA synthetase subunit beta)(A-SCS)(Succinyl-CoA synthetase beta-A chain)(SCS-betaA)
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9P2R7
-
Expression Region
53-463 aa
-
AA Sequence
LSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
-
Molecular Weight
52 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SUCLA2, or succinate-CoA ligase, is a critical enzyme involved in the metabolism of succinate, playing a significant role in the tricarboxylic acid (TCA) cycle and energy production within mitochondria. Mutations in the SUCLA2 gene can lead to succinate-CoA ligase deficiency, which is associated with severe neurological disorders, including encephalopathy and developmental delays in children. These clinical manifestations emphasize the importance of understanding the functional mechanisms of SUCLA2 and its role in mitochondrial energy metabolism. Research into SUCLA2 recombinant proteins has gained traction as scientists seek to elucidate the enzyme’s structure-function relationships, investigate its catalytic properties, and develop potential therapeutic strategies for associated disorders. By producing recombinant SUCLA2, researchers can investigate the protein's biochemical characteristics, interactions with substrates, and response to various inhibitors. This knowledge is crucial for understanding the pathogenic mechanisms underlying SUCLA2-related diseases and could pave the way for novel treatment approaches. As mitochondrial dysfunction is increasingly recognized as a contributing factor to a wide array of disorders, the study of SUCLA2 and its recombinant form could lead to broader insights into metabolic diseases, mitochondrial biology, and potential therapeutic interventions.
