Analytical Data
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Gene name
Tryptophan Synthase
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简介
The TrpA protein, especially its α subunit, plays a crucial role in catalyzing the aldol cleavage of indole glycerol phosphate to produce indole and glyceraldehyde 3-phosphate. This enzymatic activity highlights the importance of TrpA in the tryptophan biosynthetic pathway, providing an essential component of cellular processes. Tryptophan Synthase Protein, E.coli (His) is a recombinant protein dimer complex containing E. coli-derived Tryptophan Synthase protein, expressed by E. coli , with N-6*His labeled tag. Tryptophan Synthase Protein, E.coli (His), has molecular weight of 28 & 40-50 kDa, respectively.
- Application
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Alternative Names
Tryptophan synthetase; Tryptophan synthase
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Species
E.coli
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P0A877 (M1-S268)&P0A879
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Expression Region
P0A877 (M1-S268)&P0A879 (T2-I397)
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AA Sequence
MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS&TTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFINETNVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRENPDKEQLLVVNLSGRGDKDIFTVHDILKARGEI
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Molecular Weight
29&40-50 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
Tryptophan synthase is a crucial enzyme in the biosynthetic pathway of the essential amino acid tryptophan, which plays a significant role in protein synthesis, neurotransmitter production, and overall metabolic processes in various organisms, including bacteria and plants. The enzyme catalyzes the conversion of indole-3-glycerol phosphate and serine into tryptophan, making it a subject of interest for both fundamental biological research and biotechnological applications. The study of tryptophan synthase also offers insights into enzyme mechanisms and the evolution of metabolic pathways. Recombinant protein techniques have facilitated the production and characterization of tryptophan synthase, allowing researchers to manipulate its properties for various applications, including the biosynthesis of tryptophan derivatives that are valuable in pharmaceuticals and cosmetics. Understanding the structure-function relationship of this enzyme through recombinant methodologies can lead to the development of more efficient biocatalysts and the design of novel compounds that may improve human health and agricultural productivity. Moreover, the investigation of tryptophan synthase in different organisms provides comparative insights that enhance our knowledge of evolutionary biology and enzyme functionality across species.
