>95%, 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
110 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
135-140 kDa, reducing conditions
Publications
Read Publication using 1607-CD in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 250 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 CD163 Protein, CF
CD_antigen: CD163
CD163 molecule
CD163
GHI/61
HbSR
Hemoglobin scavenger receptor
M130
macrophage-associated antigen
MM130
RM3/1
SCARI1
scavenger receptor cysteine-rich type 1 protein M130
sCD163
Soluble CD163
Background
CD163, previously called M130 or p155, is a 130-160 kDa type I transmembrane glycoprotein that belongs to group B of the cysteine-rich scavenger receptor family (1-3). It is essential for clearance of hemoglobin-haptoglobin (Hb-Hp) complexes in the liver, spleen and circulation (4). The human CD163 contains a 41 amino acid (aa) signal sequence, a 1009 aa extracellular domain (ECD) with 9 scavenger receptor cysteine-rich (SRCR) domains, a 22 aa transmembrane segment, and a 39-84 aa cytoplasmic region (1). The third SRCR domain is crucial for calcium-dependent binding of hemoglobin/haptoglobin complexes (3). Three splice forms (isoforms 2, 3 and 4) vary within their intracellular regions (1, 5), while one isoform (# 4) also has a 34 aa insert between SRCR domains 5 and 6 within the ECD. While all are expressed, isoform 3 is the most abundant, being generally expressed on the cell surface and most active in endocytosis (5). An approximately 130 kDa soluble form of human CD163 (sCD163) is assumed to contain virtually all of the ECD, which shares 74%, 75%, 84%, 86%, 86% and 87% aa identity with mouse, rat, bovine, equine, porcine and canine CD163 ECD, respectively (6, 7). It is released from the cell surface by proteolysis after oxidative stress or inflammatory stimuli, including bacterial endotoxins and activation of the Toll-like receptors TLR2 or TLR5 (7-10). Expression of CD163 is constitutive, and induced by glucocorticoids, IL-10, IL-6 or endotoxin on circulating monocytes, tissue macrophages, and at low levels on monocyte-derived dendritic cells (1, 2, 11, 12). In addition to clearing Hb-Hp complexes, CD163 is also a scavenger receptor for free Hb (if Hp is depleted) and TWEAK (TNF-like weak inducer of apoptosis), and can function as an erythroblast adhesion receptor (4, 13-15).
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Sulahian, T.H. et al. (2000) Cytokine 12:1312.
Madsen, M. et al. (2004) J. Biol. Chem. 279:51561.
Kristiansen, M. et al. (2001) Nature 409:198.
Nielsen, M.J. et al. (2006) J. Leukoc. Biol. 79:837.
Moller, H.J. et al. (2002) Blood 99:378.
Droste, A. et al. (1999) Biochem. Biophys. Res. Commun. 256:110.
Hintz, K. A. et al. (2002) J. Leukoc. Biol. 72:711.
Weaver, L.K. et al. (2006) J. Leukoc. Biol. 80:26.
Timmerman, M. and P. Hogger (2005) Free Radic. Biol. Med. 39:98.
Buechler, C. et al. (2000) J. Leukoc. Biol. 67:97.
Pulford, K.A. et al. (1989) J. Clin. Pathol. 42:414.
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