Analytical Data
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Gene name
pknF
- Application
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Species
Mycobacterium tuberculosis
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WI74
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Expression Region
1-476aa
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Molecular Weight
78.1 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
The study of the recombinant protein pknF, a serine/threonine kinase, has garnered significant attention in recent years due to its potential role in various cellular processes and disease mechanisms. pknF, which is encoded by a gene found in certain bacterial species, is believed to be involved in signal transduction pathways that regulate cellular responses to environmental stresses and developmental cues. Research indicates that pknF may play a critical role in bacterial virulence, making it a potential target for novel therapeutic strategies against infectious diseases. Furthermore, the manipulation of pknF through recombinant DNA technology has enabled the production of its protein form, allowing for in-depth analysis of its biochemical properties, signaling functions, and interaction networks within cells. Understanding pknF's structure and function could provide insights into its mechanism of action and its implications in both bacterial physiology and human health. Overall, the investigation of pknF as a recombinant protein holds promise for advancing our knowledge of kinase-related pathways and developing targeted approaches in infection control and related fields.
