Recombinant Human SREC-II/SCARF2 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human SREC-II/SCARF2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Human AcLDL is immobilized at 2 µg/mL (100 µL/well), Recombinant Human SREC‑II/SCARF2 Fc Chimera (Catalog # 2527-SR) binds with an ED50 of 50.0-500 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human SREC-II/SCARF2 protein
Human SREC-II
(Gln44-Gly442)
Accession # Q96GP6
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained: Gln44 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
SCARF2
Purity
>90%, 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
  • Binding Activity
Theoretical MW
69.8 kDa (monomer).
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
86-95 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Notes

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

Alternate Names for Recombinant Human SREC-II/SCARF2 Fc Chimera Protein, CF

  • HUMZD58C02
  • SCARF2
  • scavenger receptor class F, member 2
  • Scavenger receptor expressed by endothelial cells 2 protein
  • SREC2NSR1
  • SRECII
  • SREC-II
  • SREC-IIscavenger receptor class F member 2
  • SRECRP-1
  • SREPCR

Background

The scavenger receptor (SR) family comprises a group of functionally defined membrane receptors that share a common ability to bind and internalize modified forms of low density lipoproteins (LDL) such as acetylated LDL (AcLDL) and oxidized LDL(OxLDL) (1-3). Family members are classified alphabetically. In general, they play important roles in lipid metabolism, in host defence and in the regulation of acquired immunity (2, 4). Scavenger receptor expressed by endothelial cells-I (SREC-I) and SREC-II are two proteins that belong to the F type scavenger receptor group (SR-F1 and SR-F2). The full length cDNA for human SREC-II encodes an 870 amino acid (aa) type I transmembrane protein which contains a 43 aa signal peptide, a 398 aa extracellular region, a 21 aa transmembrane segment, and a 408 aa cytoplasmic domain (5, 6). Depending upon the reference, the extracellular region contains 7-10 EGF-like repeats, with a cytoplasmic domain that is rich in serine and proline in its N-terminal half and glycine in its C-terminal segment (5, 6). There is at least one alternate splice variant that shows a 5 aa deletion in the juxtamembrane region of the cytoplasmic domain (6, 7). The deletion does not change the reading frame as the distal 390 amino acids are identical in the two isoforms. The Genbank suggests another variant is possible involving amino acids 750-768 of the precursor. Again, this doesn’t seem to change the reading frame as amino acids downstream of this are unchanged (6, 8). SREC-II is expressed by endothelial cells and vascular smooth muscle cells (5, 9). In the extracellular region human SREC-II is 95% aa identical to mouse SREC-II. The extracellular regions of human SREC-II and SREC-I are 53% aa identical. Notably, more than serving as a scavenger receptor, SREC-II would seem to form heterophilic interactions with SREC-I during cell-to-cell aggregation (5).

  1. Horiuchi, S. et al. (2003) Amino Acids 25:283.
  2. Greaves, D.R. and S. Gordon (2005) J. Lipid Res. 46:11.
  3. Platt, N. and S. Gordon (1998) Chem. Biol. 5:R193.
  4. Platt, N. and S. Gordon (2001) J. Clin. Invest. 108:649. 
  5. Ishii, J. et al. (2002) J. Biol. Chem. 277:39696.
  6. GenBank Accession # Q96GP6.
  7. GenBank Accession # NP_699165.
  8. GenBank Accession # NP_878315.
  9. Sukhanov, S. et al. (2003) Biochem. Biophys. Res. Commun. 306:443.

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Bioinformatics

Gene Symbol SCARF2
Uniprot