Analytical Data
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Gene name
F2RL2
- Application
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Alternative Names
(PAR-3)(Coagulation factor II receptor-like 2)(Thrombin receptor-like 2)
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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
O00254
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Expression Region
39-374aa
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Molecular Weight
40.0 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
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Protein Description
F2RL2, also known as protease-activated receptor 2 (PAR2), is a member of the G protein-coupled receptor family, playing a pivotal role in various physiological and pathological processes. Activated by serine proteases, F2RL2 is involved in mediating inflammatory responses, pain perception, and tissue repair mechanisms. Its dysregulation has been implicated in a range of diseases, including asthma, chronic pain, and cancer, making it an attractive therapeutic target. Recent research has focused on the recombinant production of F2RL2 to gain insights into its structure-function relationships and to develop potential pharmacological interventions. By producing F2RL2 as a recombinant protein, researchers can investigate its activation mechanisms, downstream signaling pathways, and interactions with other proteins. This understanding may lead to the design of specific inhibitors or agonists, which could offer new avenues for treating diseases associated with F2RL2 dysregulation. Furthermore, the recombinant F2RL2 can serve as a valuable tool in drug discovery and development processes, enhancing our understanding of its biological functions and therapeutic potential. Overall, the study of F2RL2 recombinant protein is an essential step toward elucidating its role in health and disease, ultimately contributing to the development of targeted therapies.
