Analytical Data
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Gene name
tnaa
- Application
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Alternative Names
tnaa；ind；Tryptophanase
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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
P0A853
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Expression Region
1-471aa
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AA Sequence
MENFKHLPEP FRIRVIEPVK RTTRAYREEA IIKSGMNPFL LDSEDVFIDL LTDSGTGAVT QSMQAAMMRG DEAYSGSRSY YALAESVKNI FGYQYTIPTH QGRGAEQIYI PVLIKKREQE KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV RNVYIKEAFD TGVRYDFKGN FDLEGLERGI EEVGPNNVPY IVATITSNSA GGQPVSLANL KAMYSIAKKY DIPVVMDSAR FAENAYFIKQ REAEYKDWTI EQITRETYKY ADMLAMSAKK DAMVPMGGLL CMKDDSFFDV YTECRTLCVV QEGFPTYGGL EGGAMERLAV GLYDGMNLDW LAYRIAQVQY LVDGLEEIGV VCQQAGGHAA FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL TIPRATYTQT HMDFIIEAFK HVKENAANIK GLTFTYEPKV LRHFTAKLKE V
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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
The research on TNAA (Tobacco Nucleotide Acid Adenine) recombinant proteins has garnered significant interest due to their potential applications in biotechnology and medicine. TNAA proteins are derived from pinyon pine and closely related species, showcasing unique properties that allow for targeted and efficient protein expression in various systems. Historically, recombinant proteins have played a pivotal role in advancing understanding of biochemical processes, vaccine development, and therapeutic interventions. With the growing demand for biopharmaceuticals, the ability to produce high yields of functional proteins is crucial. TNAA proteins offer advantages such as enhanced stability, solubility, and proper folding, which can improve their efficacy in both research and clinical settings. Furthermore, ongoing studies are exploring their applications in enzyme technology, protein engineering, and as tools for environmental sustainability. As researchers delve deeper into the structural and functional aspects of TNAA proteins, they continue to uncover novel interactions and mechanisms, paving the way for innovative applications that could transform existing paradigms in health and industry. The exploration of TNAA recombinant proteins thus represents a promising frontier in the field of molecular biology and biotechnological innovation.
