Analytical Data
-
Gene name
SDHD
- Application
-
Alternative Names
SDHD;SDH4;Succinate dehydrogenase [ubiquinone] cytochrome b small subunit. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O14521
-
Expression Region
1-159aa
-
AA Sequence
MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIH LSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALT LHGHWGLGQVVTDYVHGDALQKAAKAGLLALSALTFAGLCYFNYHDVGIC KAVAMLWKL
-
Molecular Weight
44 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
SDHD (Succinate Dehydrogenase Subunit D) is a crucial component of the mitochondrial enzyme succinate dehydrogenase, which plays a vital role in the tricarboxylic acid (TCA) cycle and the electron transport chain. Research on SDHD has gained significant attention due to its implications in various hereditary conditions, notably pheochromocytoma and paraganglioma, which are tumors arising from neural crest cells. Mutations in the SDHD gene can lead to defective enzyme activity, resulting in the accumulation of succinate, which has been associated with tumorigenesis. Additionally, the study of SDHD reconstitution proteins is critical in understanding the structural and functional dynamics of the succinate dehydrogenase complex. Investigating SDHD's role at the molecular level not only sheds light on the mechanisms of cancer development but also provides potential therapeutic targets for the treatment of SDH-related tumors. Recent advances in protein engineering and structural biology have facilitated the characterization of SDHD recombinants, offering insights into its function and interaction with other subunits in the enzyme complex. This research is pivotal, as it may lead to the development of novel strategies for diagnosis and treatment of related diseases, thus highlighting the importance of SDHD in both metabolic pathways and oncological research.











