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Recombinant Human C1qR1/CD93 His-tag Protein, CF

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Measured by its binding ability in a functional ELISA. Recombinant Human C1qR1/CD93 His-tag Protein binds to Recombinant Human IGFBP-rp1/IGFBP-7 (K95R) Protein (1334-B7) with an ED50 of 0.150-1.50 μg/mL.
Measured by its binding ability in a functional ELISA. Recombinant Human C1qR1/CD93 His-tag Protein binds to Recombinant Human IGFBP-rp1/IGFBP-7 (K95R) Protein (1334-B7) with an ED50 of 0.150-1.50 μg/mL.
2 μg/lane of Recombinant Human C1qR1/CD93 His-tag Protein (Catalog # 11587-CD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human C1qR1/CD93 His-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Recombinant Human C1qR1/CD93 His-tag binds to Recombinant Human IGFBP-rp1/IGFBP-7 (K95R) Protein (Catalog # 1334-B7) with an ED50 of 0.150-1.50 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human C1qR1/CD93 protein
Val258-Lys580 with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Val258
Protein/Peptide Type
Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
34 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
65-80 kDa, under 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 with Trehalose.
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile water.

Notes

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

Alternate Names for Recombinant Human C1qR1/CD93 His-tag Protein, CF

  • AA4 Antigen
  • C1q R1
  • C1q receptor 1
  • C1q Rp
  • C1q/MBL/SPA receptor
  • C1qR(P)
  • C1qR1
  • C1qRp
  • CD93 antigenC1qR
  • CD93 molecule
  • CD93
  • CDw93C1QR1
  • Collectin Receptor
  • Complement component 1 q subcomponent receptor 1
  • complement component 1, q subcomponent, receptor 1
  • complement component C1q receptor
  • dJ737E23.1
  • ECSM3
  • Ly68
  • Matrix-remodeling-associated protein 4
  • matrix-remodelling associated 4
  • MXRA4

Background

C1qR1, also known as CD93 and C1qRp, is an approximately 125 kDa type-1 transmembrane glycoprotein that is involved in various aspects of inflammatory reactions (1). Mature human CD93 consists of a 557 amino acid (aa) extracellular domain (ECD) containing C‑type lectin and EGF‑like domains, followed by a 21 aa transmembrane segment and a 51 aa cytoplasmic domain (2, 3). Within the ECD, human CD93 shares 65% aa sequence identity with mouse and rat CD93. CD93 is expressed by vascular endothelial cells (5) and by a variety of hematopoietic cells (3‑9). Various sized fragments of soluble CD93 (50‑75 kDa) can be shed from monocytes, neutrophils, and vascular endothelial cells following inflammatory stimulation, leaving a residual stub in the membrane (11‑13). Cross‑linking of cell surface CD93 enhances phagocytosis by monocytes and enhances the uptake of apoptotic cells in vivo (10, 15). Soluble CD93 promotes the differentiation of monocytes to macrophages, phagocytosis of apoptotic cells, and inflammatory responsiveness to multiple TLR ligands (12, 14). CD93 plays a role in cardiovascular disease progression and modulates angiogenesis, inflammation and tumor growth and its interaction with insulin-like growth factor binding protein 7 (IGFBP7) contributes to abnormal tumor vasculature (16-17).
  1. Greenlee-Wacker, M.C. et al. (2012) Curr. Drug Targets 13:411.
  2. Nepomuceno, R.R. et al. (1997) Immunity 6:119.
  3. Steinberger, P. et al. (2002) J. Leukoc. Biol. 71:133.
  4. Nepomuceno, R.R. and A.J. Tenner (1998) J. Immunol. 160:1929.
  5. McGreal, E.P. et al. (2002) J. Immunol. 168:5222.
  6. Lovik, G. et al. (2001) Scand. J. Immunol. 53:410.
  7. Danet, G.H. et al. (2002) Proc. Natl. Acad. Sci. USA 99:10441.
  8. Ikewaki, N. et al. (2010) J. Clin. Immunol. 30:723.
  9. Chevrier, S. et al. (2009) Proc. Natl. Acad. Sci. USA 106:3895.
  10. Norsworthy, P.J. et al. (2004) J. Immunol. 172:3406.
  11. Bohlson, S.S. et al. (2005) J. Immunol. 175:1239.
  12. Greenlee, M.C. et al. (2009) Inflamm. Res. 58:909.
  13. Greenlee-Wacker, M.C. et al. (2011) J. Immunol. 187:3353.
  14. Jeon, J.W. et al. (2010) J. Immunol. 185:4921.
  15. Nepomuceno, R.R. et al. (1999) J. Immunol. 162:3583.
  16. Tossetta, G. et al. (2023) Cells 12:1778.
  17. Sun, Y. et al. (2021) Sci. Transl. Med. 13:eabc8922.

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