Analytical Data
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Gene name
LTP2
- Application
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Alternative Names
Allergen Par j II Major pollen allergen Par j 2.0101 Protein P2 Allergen: Par j 2.0101
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Species
Parietaria judaica
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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
P55958
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Expression Region
32-133aa
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Molecular Weight
27.3 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
LTP2, or Lipid Transfer Protein 2, is a protein predominantly found in plants, playing a crucial role in lipid metabolism and cellular signaling. Its significance has garnered attention due to its involvement in various physiological processes, including plant defense mechanisms against pathogens and stress responses. Research into LTP2 focuses on its structure, function, and potential applications in agriculture and biotechnology. By understanding how LTP2 facilitates lipid transfer between membranes, scientists aim to unlock new strategies for enhancing crop resilience and improving seed quality. Additionally, LTP2 has been studied for its potential implications in human health, particularly in relation to allergic reactions, as some individuals may develop hypersensitivity to LTPs found in certain foods. This dual interest—both in enhancing agricultural productivity and addressing food safety concerns—has spurred investigations into the molecular mechanisms governing LTP2 activity, its interactions with other proteins, and its role in lipid signaling pathways. Through recombinant protein expression and characterization, researchers are probing its functional properties to leverage LTP2 for biotechnological innovations, promising advancements in sustainable agriculture and food science.
