Analytical Data
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Gene name
PTTG_03405
- Application
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Alternative Names
Uncharacterized protein
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Species
Puccinia triticina
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Source
Yeast
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A180GV39
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Expression Region
19-189aa
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Molecular Weight
18.7 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
PTTG_03405 is a recombinant protein of significant interest in the field of molecular biology and biotechnology. This protein, derived from specific bacterial or archaeal species, has been studied for its potential roles in various biological processes, including cell signaling, metabolism, and stress responses. It belongs to a category of proteins that are often produced through recombinant DNA technology, which allows for the expression of genes in host organisms, such as E. coli or yeast. The unique structural and functional properties of PTTG_03405 make it a valuable model for exploring protein interactions and functions, as well as for applications in enzyme development and therapeutic research. As scientists increasingly focus on understanding how proteins contribute to various cellular functions and how they can be manipulated for biotechnological applications, the study of PTTG_03405 stands to provide insights that could lead to advancements in fields such as synthetic biology, drug development, and agricultural biotechnology. Research efforts often involve determining the protein's three-dimensional structure, understanding its biochemical properties, and exploring its interactions with other biomolecules, thereby unlocking its potential for practical applications.
