Analytical Data
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Gene name
SDHAF1
- Application
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Alternative Names
SDHAF1;LYRM8;Succinate dehydrogenase assembly factor 1. 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
A6NFY7
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Expression Region
1-115aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSRHSRL QRQVLSLYRD LLRAGRGKPG AEARVRAEFR QHAGLPRSDV LRIEYLYRRG RRQLQLLRSG HATAMGAFVR PRAPTGEPGG VGSQPDDGDS PRNPHDSTGA PETRPDGR
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Molecular Weight
15 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
Related Products
Protein Description
SDHAF1, or Sucinate Dehydrogenase Assembly Factor 1, has garnered significant attention in recent years due to its crucial role in the assembly and activity of succinate dehydrogenase (SDH), an essential enzyme in the mitochondrial respiratory chain and the tricarboxylic acid (TCA) cycle. Mutations or deficiencies in SDH components, including SDHAF1, have been linked to various pathologies, particularly hereditary paragangliomas and pheochromocytomas, which are neuroendocrine tumors associated with the dysregulation of hypoxia-inducible factors and cellular metabolism. Understanding the molecular mechanisms of SDHAF1 is vital for elucidating the biochemical pathways involved in these diseases and their broader implications for mitochondrial function. Recent studies have shown that SDHAF1 facilitates the maturation of SDH by promoting the incorporation of iron-sulfur clusters, crucial for its enzymatic activity. This highlights the importance of SDHAF1 not only in basic mitochondrial biology but also as a potential therapeutic target or biomarker in cancer and metabolic disorders. Exploring the structural and functional properties of SDHAF1 through recombination techniques is essential for advancing our knowledge of its role in SDH assembly and to develop strategies aimed at correcting the dysfunctions arising from its loss. As research progresses, the focus on recombinant SDHAF1 proteins may provide new insights into targeted treatments and interventions in related diseases, underscoring the protein's significance in both health and disease contexts.
