Recombinant Human C1qR1/CD93 (24-580) His Avi Protein, CF New
Recombinant Human C1qR1/CD93 (24-580) His Avi Protein, CF Summary
- R&D Systems HEK293-derived Recombinant Human C1qR1/CD93 (24-580) His Avi Protein (AVI11656)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
Ala24-Lys580, with a C-terminal 6-His tag and Avi-tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AVI11656
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 200 μg/mL in water. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human C1qR1/CD93 (24-580) His-tag Avi-tag Protein (Catalog # AVI11656) binds to Recombinant Human IGFBP-rp1/IGFBP-7 (K95R) Protein (1334-B7) with an ED50 of 1.50‑15.0 μg/mL.
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2 μg/lane of Biotinylated Recombinant Human C1qR1/CD93 (24-580) His-tag Avi-tag Protein (Catalog # AVI11656) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 82-105 kDa.
Reconstitution Calculator
Background: C1qR1/CD93
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). Our Avi-tag Biotinylated Human C1qR1/CD93 (24-580) features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Greenlee-Wacker, M.C. et al. (2012) Curr. Drug Targets 13:411.
- Nepomuceno, R.R. et al. (1997) Immunity 6:119.
- Steinberger, P. et al. (2002) J. Leukoc. Biol. 71:133.
- Nepomuceno, R.R. and A.J. Tenner (1998) J. Immunol. 160:1929.
- McGreal, E.P. et al. (2002) J. Immunol. 168:5222.
- Lovik, G. et al. (2001) Scand. J. Immunol. 53:410.
- Danet, G.H. et al. (2002) Proc. Natl. Acad. Sci. USA 99:10441.
- Ikewaki, N. et al. (2010) J. Clin. Immunol. 30:723.
- Chevrier, S. et al. (2009) Proc. Natl. Acad. Sci. USA 106:3895.
- Norsworthy, P.J. et al. (2004) J. Immunol. 172:3406.
- Bohlson, S.S. et al. (2005) J. Immunol. 175:1239.
- Greenlee, M.C. et al. (2009) Inflamm. Res. 58:909.
- Greenlee-Wacker, M.C. et al. (2011) J. Immunol. 187:3353.
- Jeon, J.W. et al. (2010) J. Immunol. 185:4921.
- Nepomuceno, R.R. et al. (1999) J. Immunol. 162:3583.
- Tossetta, G. et al. (2023) Cells 12:1778.
- Sun, Y. et al. (2021) Sci. Transl. Med. 13:eabc8922.
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