Analytical Data
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Gene name
SDHAF2
- Application
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Alternative Names
SDHAF2;C11orf79;PGL2;SDH5;Succinate dehydrogenase assembly factor 2. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NX18
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Expression Region
30-166aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSSFRRFYR GDSPTDSQKD MIEIPLPPWQ ERTDESIETK RARLLYESRK RGMLENCILL SLFAKEHLQH MTEKQLNLYD RLINEPSNDW DIYYWATEAK PAPEIFENEV MALLRDFAKN KNKEQRLRAP DLEYLFEKPR
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Molecular Weight
19 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
SDHAF2, or succinate dehydrogenase assembly factor 2, has emerged as a critical protein in the context of mitochondrial biology and cellular metabolism. It plays an essential role in the assembly and maturation of succinate dehydrogenase (SDH), a key enzyme complex in the mitochondrial respiratory chain that links the tricarboxylic acid cycle to oxidative phosphorylation. Dysfunctions in SDH and its assembly factors, including SDHAF2, have been implicated in various metabolic disorders and cancers, particularly in tumors characterized by mitochondrial dysfunction. Thus, understanding the mechanism of SDHAF2 and its interactions within the assembly of SDH is crucial for elucidating the pathophysiology of these conditions. Recent studies have highlighted the importance of SDHAF2 not only in enzyme assembly but also in maintaining mitochondrial integrity and function. Targeting SDHAF2 may provide new therapeutic avenues for diseases linked to mitochondrial dysfunction. Furthermore, the exploration of its structure, interaction partners, and regulatory mechanisms is vital for the potential development of molecular interventions aimed at restoring normal SDH function in affected tissues. Ongoing research on SDHAF2 thus represents a promising frontier in both cancer biology and metabolic research, warranting further investigation into its molecular roles and therapeutic potential.
