Recombinant Mouse PLA2R1 Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse PLA2R1 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA.

  When Recombinant Human PLA2G1B (Catalog # 5018-PL) is immobilized at 5 μg/mL (100 μL/well), the concentration of Recombinant Mouse PLA2R1 that produces 50% of the optimal binding response is found to be approximately 1.5-7.5 μg/mL.

• Source: Mouse myeloma cell line, NS0-derived mouse PLA2R1 protein
  Gln27-Gly1392, with a C-terminal 6-His tag
• Accession #: NP_032893
• N-terminal Sequence: No results obtained: Gln27 predicted (N-sequencing might be blocked)
• Protein/Peptide Type: Recombinant Proteins
• Gene: Pla2r1
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 157.5 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 150-170 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse PLA2R1 Protein, CF

• 180 kDa secretory phospholipase A2 receptor
• CLEC13C
• CLEC13CC-type lectin domain family 13 member C
• phospholipase A2 receptor 1, 180kDa
• PLA2G1R
• PLA2IR
• PLA2R1
• PLA2-RM-type receptor
• PLA2Rphospholipase A2 receptor 1, 180kD
• secretory phospholipase A2 receptor

Background

PLA2R1 (phospholipase A2 receptor 1) also called muscle (M-)type PLA2R or secretory (s)PLA2R is a 180-200 kDa type I transmembrane glycoprotein that is a member of subgroup VI of the C-type lectin superfamily (1-3). The 1487 amino acid (aa) mouse PLA2R1 contains a 26 aa signal sequence, a 1370 aa ECD, a 21 aa transmembrane sequence, and a 70 aa cytoplasmic domain with an endocytosis motif. The ECD contains one ricin B-type lectin domain (aa 42-165), a fibronectin type II region (aa 176-224), and eight C-type lectin carbohydrate recognition domains (CRDs, aa 241-1377) (1-3). CRDs 3-5 are the major PLA2 binding site (1, 3). The mouse PLA2R1 ECD shares 75% and 86% aa identity with human and rat PLA2R1, respectively. One isoform shows a 35 aa N-terminal extension, and a potentially secreted isoform contains a 10 aa substitution for aa 680-1487 (4). Matrix metalloproteinases can generate a 180 kDa soluble inhibitory form in mouse serum that retains PLA2 binding activity (3, 5). Mouse PLA2R1 is widely expressed, including on type II alveolar cells, neutrophils and mast cells, and binds mouse secretory PLA2s IB, IIA, IIE, IIF and X, and snake venom PLAs (1-3, 5-8). Among mammals, PLA2R1 ligand recognition is mainly species‑specific (3). PLA2R1 can be anti‑inflammatory by inhibiting PLA2‑induced release lipid mediators such as arachadonic acid (5  7, 9). PLA2R1 can also mediate internalization and clearance of PLA2s (10). PLA2R1 can also be pro‑inflammatory, and its deletion in mouse reduces susceptibility to LPS-induced endotoxic shock (8). Engagement activates the MAPK/ERK signaling pathway and enhances pro-inflammatory cytokine release (6, 8, 11). PLA2 binding can stimulate cell adhesion, proliferation or senescence, neutrophil elastase release, and smooth muscle contraction (6, 9, 12). All PLA2R1 intracellular signaling is largely independent of ligand phospholipase activity (6, 11).

1. Higashino, K-I. et al. (1994) Eur. J. Biochem. 225:375.
2. Lambeau, G. et al. (1994) J. Biol. Chem. 269:1575.
3. Hanasaki, K. (2004) Biol. Pharm. Bull. 27:1165.
4. SwissProt Accession Q62028.
5. Higashino, K-I. et al. (2002) J. Biol. Chem. 277:13583.
6. Silliman, C.C. et al. (2002) Am. J. Physiol. Cell Physiol. 283:C1102.
7. Rouault, M. et al. (2007) Biochemistry 46:1647.
8. Hanasaki, K. et al. (1997) Biol. Chem. 272:32792.
9. Ancian, P. et al. (1995) Biochemistry 34:13146.
10. Yokota, Y. et al. (2001) FEBS Lett. 509:250.
11. Granata, F. et al. (2005) J. Immunol. 174:464.
12. Augert, A. et al. (2009) EMBO Rep. 10:271.

Bioinformatics

• Gene Symbol: Pla2r1
• Uniprot:
  • NP_032893()