Analytical Data
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Gene name
TLL1
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43897
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Expression Region
Asp730~Ile1003
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Molecular Weight
39kDa
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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
TLL1 (thrombin-like protein 1) is a member of the serine protease family, and its exploration has garnered significant attention due to its potential implications in both physiological and pathological processes. Initially discovered in the context of various biological systems, TLL1 plays a crucial role in extracellular matrix remodeling, cell signaling, and wound healing. Its unique enzymatic properties allow it to modulate other proteins, influencing various cellular functions. Additionally, studies have shown that TLL1 may be involved in the progression of certain diseases, including cancer and cardiovascular disorders, where aberrant protease activity can lead to adverse effects. The recombinant production of TLL1 has enabled researchers to investigate its structure-function relationships, paving the way for a deeper understanding of its biological roles. Moreover, the availability of TLL1 as a recombinant protein facilitates high-throughput screenings and therapeutic applications, including its potential use in drug development and biotechnological applications. Overall, research on TLL1 and its recombinant forms promises to enhance our comprehension of proteolytic mechanisms and may lead to novel therapeutic strategies for various diseases.
