Analytical Data
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Gene name
THFA
- Application
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Alternative Names
THFA；HSPOX1；HYPDH；Hydroxyproline dehydrogenase
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Species
Mouse
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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
Q8VCZ9
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Expression Region
1-456aa
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AA Sequence
MIWTRLPLYG PSKPSTGGWQ PLRFDGGAFH VKGTAELARA LLVLRLCAWP PLVTHGLAFQ AWSQRLLGSR LSGALLRASI YGQFVAGETA EEVRNCVGQL QALGLQPLLA VPTEEEPDST AKTSEVWYEE NLSAMLRCVD LSRALVDAHG PARNSLMQLK VTALASTRLC KELSAWIQRP RGSSELSPER LAEAMDSGRN LQLSCLSTEQ NQHLQASLSR LHRVAQHARA KCVRLLVDAE YTFINPALSL LVAALAVRWN SPEEGGPWVW NTYQAYLKDT HQRLEQDAEA AHKAGLAFGV KLVRGAYLDK ERSMTQLQGK EDCTQPDYEA TSRSYSRCLE LMLRCVSNHG PPCHLMVASH NEESVRQATK RMWELGIPLD GPVCFGQLLG MCDHVSLALG QAGYMVYKSI PYGCLEEVIP YLIRRAQENR SVLQGARREQ ALLSQELWRR LLGRTA
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Molecular Weight
50.7 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
THFA (Tetrahydrofolate) is a crucial cofactor in various enzymatic reactions, particularly those involved in one-carbon metabolism and the synthesis of nucleotides and amino acids. Its importance spans diverse biological processes, including DNA synthesis and repair, making it essential for cellular growth and division. Researchers have increasingly focused on the study of THFA and its recombinant protein forms to enhance our understanding of its functional roles in metabolic pathways and its potential applications in medicine and biotechnology. Recombinant THFA proteins can be utilized to dissect enzymatic mechanisms, explore metabolic disorders related to folate metabolism, and develop novel therapeutic strategies for conditions like cancer or neurological disorders where one-carbon metabolism is disrupted. By producing these proteins through recombinant DNA technology, scientists can achieve high yields and purities, facilitating detailed biochemical and structural studies. Moreover, investigating THFA's interactions with various enzymes and substrates will provide insights into its regulatory functions and contribute to the development of targeted therapies that leverage these pathways. Overall, THFA recombinant protein research is poised to illuminate significant aspects of cellular metabolism and open new avenues for therapeutic intervention.
