Analytical Data
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Gene name
TRY1
- Application
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Alternative Names
Alpha-trypsin chain 2; Beta-trypsin; Cationic trypsinogen; Digestive zymogen; Nonfunctional trypsin 1; Prss1; Serine protease 1; TCR V beta 4.1; TRP1; TRY1; TRY1_HUMAN; TRY4; TRYP1; Trypsin I; Trypsinogen 1; Trypsinogen A
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Species
Human
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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
P07477
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Expression Region
24-247 aa
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AA Sequence
IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS
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Molecular Weight
31.6 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
TRY1 is a member of the plant tryptophan-rich proteins family, which play crucial roles in various physiological processes, including plant development, stress responses, and defense mechanisms. The research on TRY1 is driven by its potential applications in improving crop resilience and enhancing agricultural productivity in the face of climate change and increasing pest pressures. Understanding the structure and function of TRY1 can provide insights into its role in plant signaling pathways and stress tolerance mechanisms. Moreover, as global food security becomes a pressing issue, exploring the molecular characteristics of such proteins could lead to the development of genetically engineered plants with enhanced traits. By utilizing advanced molecular biology techniques, researchers aim to elucidate the functional properties of TRY1, investigate its interaction with other biomolecules, and assess its effectiveness in transgenic models. This research not only contributes to basic plant biology but also has significant implications for sustainable agriculture and food production. Through a deeper understanding of TRY1, scientists hope to pave the way for the development of innovative strategies to cultivate crops that thrive in challenging environmental conditions, ultimately supporting food security efforts worldwide.
