Analytical Data
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Gene name
PAR2
- Application
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Alternative Names
GPR11; PAR2
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Species
Human
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Source
Baculovirus
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Tag
His;Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P55085
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Expression Region
V55-L269, E276-K377, G89A, H108A, G157A, M166L, Y174A, V176E, N222Q, M268A, I289A, L293A
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Protein Length
Partial
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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
PAR2 (Protease-Activated Receptor 2) is a G-protein coupled receptor that plays a significant role in various physiological processes, such as inflammation, pain sensation, and tissue homeostasis. Unlike traditional receptors, PAR2 is activated by proteolytic cleavage, primarily by serine proteases like trypsin and mast cell chymase, which reveals a new N-terminus that acts as a tethered ligand. This unique mechanism of activation allows PAR2 to mediate cellular responses in the context of numerous pathologies, including asthma, arthritis, and cancer. Research into PAR2 has gained momentum due to its potential as a therapeutic target, with compounds that can either activate or inhibit its signaling pathways eliciting considerable interest. Furthermore, understanding the molecular dynamics and structural characteristics of PAR2 through recombinant protein studies has provided insights into its function and interactions with other signaling molecules. Such studies are crucial for designing specific modulators that can fine-tune PAR2 activity in various disease states, ultimately aiming to improve therapeutic strategies for conditions exacerbated by dysregulated PAR2 signaling.











