Analytical Data
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Gene name
EPSPS1
- Application
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Alternative Names
EPSPS1；3-phosphoshikimate 1-carboxyvinyltransferase
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Species
E.coli
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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
W0FAR5
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Expression Region
1-332aa
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AA Sequence
AAGGNASYVLDGVPRMRERPIGDLVAGLKQLGADVDCFMGTNCPPVRVNAMGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIIDKLISIPYVEMTLKLMERFGVKVEHSDNWDRFYIKGAQKYKSPGNAYVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAKVSWTENSVTVTGPPRDPSKKGHLRGIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMVAICTELRKLGATVEEGPDFCIITPPEKLNITAIDTYDDHRMAMAFSIAACADVPVTIRDPGCTRKTFPDYFDVLQRFTKH
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Molecular Weight
35.6 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
The EPSPS1 (5-enolpyruvylshikimate-3-phosphate synthase 1) protein is a key enzyme in the shikimic acid pathway, which is vital for the biosynthesis of aromatic amino acids in plants, microorganisms, and fungi. This pathway is not present in animals, making EPSPS1 an important target for agricultural biotechnology and herbicide development. The enzyme functions in catalyzing the reaction between phosphoenolpyruvate and shikimate-3-phosphate, leading to the synthesis of shikimate-5-phosphate. Research into EPSPS1 has gained momentum due to the emergence of glyphosate-resistant weed species, necessitating a deeper understanding of the enzyme's structure, function, and potential modifications to enhance herbicide efficacy. Advances in recombinant protein technology have enabled the production of EPSPS1 in heterologous systems for detailed biochemical and structural studies. These investigations aim to elucidate the enzyme's mechanisms, interactions with substrate and inhibitors, and the genetic basis for herbicide resistance. Furthermore, exploring the evolutionary aspects of EPSPS1 across different species can provide insights into its adaptive significance and potential applications in crop protection. Understanding the nuances of EPSPS1 can lead to novel approaches in developing sustainable agricultural practices while minimizing environmental impact.
