Analytical Data
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Gene name
FAHD1
- Application
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Alternative Names
Acylpyruvase FAHD1; C16orf36; Chromosome 16 open reading frame 36; DKFZP566J2046; FAHD1; FAHD1_HUMAN; Fumarylacetoacetate hydrolase domain containing protein 1; Fumarylacetoacetate hydrolase domain-containing protein 1; MGC74876; mitochondrial; YISK like; YISK like/RJD15; YisK-like protein; YISKL
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6P587
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Expression Region
1-47aa
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AA Sequence
MFQITFRCLPNFLRFGHHQEAFVKIKISTNYWPISDLLNQFDRINLQ
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Molecular Weight
32.1 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
FAHD1, or fatty acid hydrolase domain-containing protein 1, has emerged as a significant focus of research due to its potential role in various biological processes and its implications in metabolic disorders. Initially identified through genomic studies, FAHD1 is presumed to be involved in fatty acid metabolism, influencing energy homeostasis and lipid storage. Various studies have suggested that dysregulation of FAHD1 expression may correlate with conditions such as obesity, diabetes, and cardiovascular diseases. The protein’s unique structure, characterized by a hydrolase domain, enables it to interact with various substrates, making it a potential target for therapeutic interventions. Recent advances in recombinant protein technology have facilitated the expression and purification of FAHD1, allowing researchers to explore its enzymatic properties and functional roles in greater detail. Furthermore, understanding the molecular mechanisms governing FAHD1 activity could pave the way for novel strategies in managing metabolic disorders. As research progresses, FAHD1 is positioned as a promising candidate for further investigation within the scope of metabolic health and disease prevention, highlighting the need for comprehensive studies to elucidate its physiological significance and potential applications in biomedical science.
