Recombinant Human M-CSF R/CD115 Fc Avi-tag Protein, CF Summary
| Additional Information |
Biotinylated |
| Details of Functionality |
The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. Measured by its binding ability in a functional ELISA. When Human M-CSF (Catalog # 216-MC) is immobilized at 1 µg/mL (100 µL/well), it binds to Biotinylated Recombinant Human M-CSF R/CD115 Fc Chimera Avi-tag (Catalog # AVI10339) with an ED 50 of 6-36 ng/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human M-CSF R/CD115 protein | Human M-CSF R/CD115 (Ile20-Thr516) Accession # P07333.2 | IEGRMD | Human IgG 1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
| Accession # |
|
| N-terminal Sequence |
Ile20 |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>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 |
|
| Theoretical MW |
83 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 |
100-120 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 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 with Trehalose. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human M-CSF R/CD115 Fc Avi-tag Protein, CF
Background
M-CSF receptor, the product of the
c-
fms proto-oncogene, is a member of the type III subfamily of receptor tyrosine kinases that also includes receptors for SCF and PDGF. These receptors each contain five immunoglobulin-like domains in their extracellular domain (ECD) and a split kinase domain in their intracellular region (1-4). M-CSF receptor is expressed primarily on cells of the monocyte/macrophage lineage, dendritic cells, stem cells and in the developing placenta (1). Human M-CSF receptor cDNA encodes a 972 amino acid (aa) type I membrane protein with a 19 aa signal peptide, a 493 aa extracellular region containing the ligand-binding domain, a 25 aa transmembrane domain and a 435 aa cytoplasmic domain. The human M-CSF R ECD shares 60%, 64%, 72%, 75%, 75% and 76% aa identity with mouse, rat, bovine, canine, feline and equine M-CSF R, respectively. Activators of protein kinase C induce TACE/ADAM17 cleavage of the M-CSF receptor, releasing the functional ligand-binding extracellular domain (5). M-CSF binding induces receptor homodimerization, resulting in transphosphorylation of specific cytoplasmic tyrosine residues and signal transduction (6). The intracellular domain of activated M-CSF R binds more than 150 proteins that affect cell proliferation, survival, differentiation and cytoskeletal reorganization. Among these, PI3Kinase, P42/44 ERK and c-Cbl are key transducers of M-CSF R signals (3, 4). M-CSF R engagement is continuously required for macrophage survival and regulates lineage decisions and maturation of monocytes, macrophages, osteoclasts and DC (3, 4). M-CSF R and integrin alpha v beta 3 share signaling pathways during osteoclastogenesis and deletion of either causes osteopetrosis (7, 8). In the brain, microglia expressing increased M-CSF R are concentrated with Alzheimers a beta peptide, but their role in pathogenesis is unclear (9, 10).
- deParseval, N. et al. (1993) Nucleic Acids Res. 21:750.
- Rothwell, V.M. and L.R. Rohrschneider (1987) Oncogene Res. 1:311.
- Chitu, V. and E.R. Stanley (2006) Curr. Opin. Immunol. 18:39.
- Ross, F.P. and S.L. Teitelbaum (2005) Immunol. Rev. 208:88.
- Rovida, E. et al. (2001) J. Immunol. 166:1583.
- Yeung, Y. et al. (1998) J. Biol. Chem. 273:17128.
- Dai, X. et al. (2002) Blood 99:111.
- Faccio, R. et al. (2003) J. Clin. Invest. 111:749.
- Li, M. et al. (2004) J. Neurochem. 91:623.
- Mitrasinovic, O.M. et al. (2005) J. Neurosci. 25:4442.
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