Recombinant Human SREC-I/SCARF1 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‑I/SCARF1 Fc Chimera (Catalog # 2409-SR) binds with an ED50 of 5.00-50.0 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human SREC-I/SCARF1 protein
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
69.1 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
100 kDa, reducing conditions
Publications
Read Publications using 2409-SR in the following applications:
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
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human SREC-I/SCARF1 Fc Chimera Protein, CF
Acetyl LDL receptor
KIAA0149endothelial cells scavenger receptor
MGC47738
SCARF1
scavenger receptor class F, member 1
Scavenger receptor expressed by endothelial cells 1
SREC1
SRECI
SREC-I
SRECscavenger receptor expressed by endothelial cells
SR-F1
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. 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 of human SREC-I encodes an 830 amino acid (aa) type I transmembrane protein which contains a 19 aa signal peptide, a 402 aa extracellular region, a 21 aa transmembrane segment, and a 388 aa long cytoplasmic domain. The extracellular region contains ten EGF-like repeats (five of which fit the exact consensus sequence for an EGF-like domain) while the cytoplasmic domain is rich in serine and proline in the N-terminal half, and glycine in the C-terminal segment (5, 6). In addition to the full length form, four SREC-I isoforms exist. Two show insertions of a stop codon in EGF-like domain #8, resulting in mature soluble forms of 323 aa and 318 aa, respectively. A third isoform deletes part of domain #8 plus domains #9 and #10; it continues in-frame to generate a mature transmembrane protein of 725 aa. The last isoform shows only cytoplasmic splicing, with 72 aa substituted for the last 332 aa of the full length form. All three transmembrane forms bind acetylated LDL (6). Native SREC-I is approximately 150 kDa in size, and expressed by endothelial cells, macrophages and fetal neurons (7, 8). In the extracellular region human SREC-I is 76% aa identical to mouse SREC-I. The extracellular regions of human SREC-I and II are 53% aa identical.
Horiuchi, S. et al. (2003) Amino Acids 25:283.
Greaves, D.R. and S. Gordon (2005) J. Lipid Res. 46:11.
Platt, N. and S. Gordon (1998) Chem. Biol. 5:R193.
Platt, N. and S. Gordon (2001) J. Clin. Invest. 108:649.
Adachi, H. et al. (1997) J. Biol. Chem. 272:31217.
Adachi, H. and M. Tsujimoto (2002) J. Biol. Chem. 277:24014.
Shibata, M. et al. (2004) J. Biol. Chem. 279:40084.
Tanura, Y. et al. (2004) J. Biol. Chem. 279:30938.
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