表达区间及表达系统(Source)
Human PAR2 Full Length Protein (VLP) (PA2-H52P7) is expressed from human 293 cells (HEK293). It contains AA Ser 37 - Tyr 397 (Accession # P55085).
Predicted N-terminus: Asp
蛋白结构(Molecular Characterization)
The protein has a calculated MW of 84.8 kDa | 56.1 kDa.
Virus-like particles(VLPs) are formed by self-assembly of envelop/capsid proteins from viruses. Membrane Proteins can be constituted in-situ with VLPs produced from HEK293 cell cultures. These VLPs concentrate conformationally intact membrane proteins directly on the cell surface and produce soluble, high-concentration proteins perfect for immunization and antibody screening.
The VLPs provide the display of properly folded membrane proteins in their native cellular membrane in a compact size of 100~300 nm diameter (similar to the size of most viruses) making it optimal targets for dendritic cells in vivo and surface attachment for phage display.
内毒素(Endotoxin)
Less than 1.0 EU per μg by the LAL method.
制剂(Formulation)
The VLPs are highly immunogenic, so the immunization strategy should be optimized (antigen dose, regimen and adjuvant).
Supplied as 0.2 μm filtered solution in PBS, Arginine, pH7.4 with trehalose as protectant.
Contact us for customized product form or formulation.
运输(Shipping)
This product is supplied and shipped with dry ice, please inquire the shipping cost.
存储(Storage)
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- The product MUST be stored at -70°C or lower upon receipt;
- -70°C for 12 months under sterile conditions.
活性(Bioactivity)-ELISA
Immobilized Human PAR2 Full Length Protein (VLP) (Cat. No. PA2-H52P7) at 5 μg/mL (100 μL/well) can bind Anti-PAR2 Antibody, Human IgG1 with a linear range of 1-39 ng/mL (QC tested).
Protocol
均一性(Identity)-DLS
The mean peak Radius of VLP is 60-80 nm with more than 95% intensity as determined by dynamic light scattering (DLS).
背景(Background)
This gene encodes a member of the G-protein coupled receptor 1 family of proteins. The encoded cell surface receptor is activated through proteolytic cleavage of its extracellular amino terminus, resulting in a new amino terminus that acts as a tethered ligand that binds to an extracellular loop domain. Activation of the receptor has been shown to stimulate vascular smooth muscle relaxation, dilate blood vessels, increase blood flow, and lower blood pressure. This protein is also important in the inflammatory response, as well as innate and adaptive immunity. [provided by RefSeq, Jun 2016]