roduct Information
| Property | Description |
|---|---|
| Product Name | Anti-human PAR1 Recombinant Monoclonal Antibody |
| Antibody ID | HM0087 |
| Target Protein | Proteinase-activated receptor 1 |
| Target Protein Short Name | PAR1 |
| UniProt Accession | P25116 |
| Molecular Weight | Human: 47.4 kDa |
| Antibody Type | Recombinant monoclonal antibody |
| Host Species | Mouse |
| Recombinant Format | Full-length mouse IgG1 |
| Isotype | Mouse IgG1 |
| Species Reactivity | Human |
| Tested Applications | WB |
| Recommended Dilution for WB | 1:500–1:5000 |
| Antigen | Recombinant epitope-Fc fusion protein |
| Epitope Sequence | NPNDKYEPFWEDEEKNESGLTE |
| Expression System | HEK293 cells |
| Purification | Protein G affinity chromatography |
| Conjugate | Unconjugated |
| Concentration | 0.1 mg/mL |
| Storage Buffer | 0.1 M Tris, 0.05 M Glycine, 0.07 M NaCl, 2 g/L BSA, 50% glycerol, pH 7 |
| Storage Condition | Store at -20°C |
| Research Use | For research use only. Not for diagnostic or therapeutic applications |
Product Background
PAR1 (Proteinase-activated receptor 1), also known as F2R, is a G protein-coupled receptor activated by proteolytic cleavage, primarily by thrombin. PAR1 regulates platelet activation, coagulation signaling, endothelial function, inflammation, vascular biology, cancer progression, and cellular signaling pathways.
PAR1 is widely studied in thrombosis research, cardiovascular biology, inflammation, GPCR signaling, cancer biology, endothelial signaling, platelet biology, and receptor pharmacology.
Antibody Development
HM0087 was generated by phage-display selection using a mouse-derived antibody library. Recombinant epitope-Fc fusion protein containing the PAR1 epitope sequence was used as the selection antigen. Following identification of the initial antibody candidate, structure-guided affinity optimization was performed to improve binding affinity and specificity.
The optimized antibody was reconstructed as a full-length mouse IgG1 recombinant antibody and expressed in HEK293 cells.
Binding and specificity were evaluated by:
- ELISA using recombinant epitope-Fc fusion antigen
- Western blot detection of endogenous full-length PAR1 protein
Validation Data
ELISA Validation
ELISA demonstrated specific binding to recombinant epitope-Fc fusion antigen, while minimal binding was observed against Fc control protein.
Validation conditions:
- Well 1: Fc control protein
- Well 2: Epitope-Fc fusion protein
- Detection substrate: TMB
Note:
ELISA validation confirms binding to the epitope-Fc fusion antigen. Full-length PAR1 protein binding in solution has not been tested by ELISA.
Western Blot Validation – Recombinant Fusion Protein
Western blot analysis demonstrated specific recognition of recombinant MBP-epitope fusion protein expressed in BL21(DE3) cells, while no significant binding was observed against MBP control protein.
Validation conditions:
- Lane 1: MBP control protein
- Lane 2: MBP-epitope fusion protein
- Standard reducing Western blot
Western Blot Validation – Endogenous Full-Length Protein
Western blot analysis detected endogenous full-length PAR1 protein under reducing conditions.
Validated samples:
- 293T cells
- HeLa cells
- HepG2 cells
Detection condition:
- Standard reducing Western blot
- HRP-conjugated anti-mouse secondary antibody
Observed bands:
- Clear bands observed near the expected molecular weight range for endogenous PAR1 protein
Additional bands may represent receptor oligomers, glycosylated receptor species, receptor processing intermediates, or post-translationally modified receptor forms commonly observed for GPCR proteins under reducing Western blot conditions.















