Analytical Data
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Gene name
PAR2
- Application
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Alternative Names
PAR2；GPR11；PAR2；Proteinase-activated receptor 2
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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
O75469
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Expression Region
1-434aa
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AA Sequence
MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEERRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSSGCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLLPHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWECGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHRVVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPFATPLMQELFGITGS
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Molecular Weight
69.8kDa
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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
PAR2 (Proteinase-Activated Receptor 2) is a G protein-coupled receptor that plays a pivotal role in various physiological and pathological processes, including inflammation, pain sensation, and tissue repair. It is activated by serine proteases, such as trypsin and mast cell tryptase, which cleave the receptor’s N-terminal domain, leading to a conformational change that initiates intracellular signaling pathways. Research on PAR2 has gained traction due to its involvement in the modulation of pain and itch, particularly in chronic pain conditions where traditional analgesics often fall short. Moreover, PAR2 has been implicated in various diseases, including asthma, arthritis, and cancer, highlighting its potential as a therapeutic target. The recombinant expression of PAR2 allows for detailed studies of its structure, function, and interaction with ligands. Understanding the molecular mechanisms of PAR2 signaling can pave the way for novel approaches in drug development to target PAR2 for therapeutic benefit in chronic inflammatory diseases and pain management. As such, the study of PAR2 recombinant proteins not only enhances our fundamental understanding of this receptor but also offers insights into innovative treatment strategies for a range of debilitating conditions.
