Analytical Data
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Gene name
Trigger factor
- Application
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Alternative Names
PPIase
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Species
Escherichia coli O127:H6
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
B7UJQ9
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Expression Region
1-432aa
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Molecular Weight
64.2 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
Trigger factor (TF) is a highly conserved chaperone protein found in bacteria and organelles of eukaryotic cells, playing a vital role in protein folding and stabilization. It binds to nascent polypeptide chains emerging from the ribosome, preventing misfolding and aggregation, which is crucial in maintaining cellular protein homeostasis. Research into TF has gained momentum due to its potential implications in understanding protein synthesis and folding mechanisms, as well as its role in stress responses. The importance of TF extends beyond mere chaperoning; it has been implicated in various cellular processes, including assisting in the proper folding of multi-domain proteins and facilitating the assembly of protein complexes. Moreover, TF has been recognized for its potential in developing biotechnological applications, such as enhancing the yield of recombinant proteins in microbial systems. Recent studies have focused on elucidating the structural and functional properties of TF, exploring its interactions with various substrates, and understanding its regulation under physiological and stress conditions. As researchers aim to harness the capabilities of TF in different contexts, including therapeutics and industrial biotechnology, the exploration of recombinant TF continues to offer insights into its chaperone mechanics and potential applications in enhancing protein production and quality.
