Recombinant Human M-CSF Biotinylated Protein, CF

When Recombinant Human M-CSF R/CD115 Fc Chimera Protein (329-MR) is immobilized at 0.5 μg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human M‑CSF Protein (Catalog # BT216) that produces 50% of the optimal binding response is 1.50-15.0 ng/mL.

2 μg/lane of Biotinylated Recombinant Human M‑CSF Protein (Catalog # BT216) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 15-22 kDa and 30-40 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human M-CSF Biotinylated Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human M-CSF R/CD115 Fc Chimera Protein (Catalog # 329-MR) is immobilized at 0.5 μg/mL (100 µL/well), the concentration of &Biotinylated Recombinant Human M‑CSF (Catalog # BT216) that produces 50% of the optimal binding response is 1.50‑15.0 ng/mL.
• Source: E. coli-derived human M-CSF protein
  Glu33-Ser190, with an N-terminal Met
• Accession #: NP_757350.2
• N-terminal Sequence: Met
• Structure / Form: Disulfide-linked homodimer
  Biotinylated via amines
• 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:
  • Bioactivity
• Theoretical MW: 18.5 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: 15-22 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 °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 with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 250 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 Biotinylated Protein, CF

• colony stimulating factor 1 (macrophage)
• CSF1
• CSF-1
• Lanimostim
• macrophage colony stimulating factor
• macrophage colony-stimulating factor 1
• MCSF
• M-CSF
• MCSFlanimostim
• MGC31930

Background

M-CSF, also known as CSF-1, is a four-alpha -helical-bundle cytokine that is the primary regulator of macrophage survival, proliferation and differentiation (1-3). M-CSF is also essential for the survival and proliferation of osteoclast progenitors (1, 4). M-CSF also primes and enhances macrophage killing of tumor cells and microorganisms, regulates the release of cytokines and other inflammatory modulators from macrophages, and stimulates pinocytosis (2, 3). M-CSF increases during pregnancy to support implantation and growth of the decidua and placenta (5). Sources of M-CSF include fibroblasts, activated macrophages, endometrial secretory epithelium, bone marrow stromal cells and activated endothelial cells (1-5). The M-CSF receptor (c-fms) transduces its pleotropic effects and mediates its endocytosis. M-CSF mRNAs of various sizes occur (3-9). Full length human M-CSF transcripts encode a 522 amino acid (aa) type I transmembrane (TM) protein with a 464 aa extracellular region, a 21 aa TM domain, and a 37 aa cytoplasmic tail that forms a 140 kDa covalent dimer. Differential processing produces two proteolytically cleaved, secreted dimers. One is an N- and O- glycosylated 86 kDa dimer, while the other is modified by both glycosylation and chondroitin-sulfate proteoglycan (PG) to generate a 200 kDa subunit. Although PG-modified M-CSF can circulate, it may be immobilized by attachment to type V collagen (8). Shorter transcripts encode
M‑CSF that lacks cleavage and PG sites and produces an N-glycosylated 68 kDa TM dimer and a slowly produced 44 kDa secreted dimer (7). Although forms may vary in activity and half-life, all contain the N‑terminal 150 aa portion that is necessary and sufficient for interaction with the M-CSF receptor (10, 11). The first 223 aa of mature human M-CSF shares 88%, 86%, 81% and 74% aa identity with corresponding regions of dog, cow, mouse and rat M‑CSF, respectively (12, 13). Human M-CSF is active in the mouse, but mouse M-CSF is reported to be species-specific.

1. Pixley, F.J. and E.R. Stanley (2004) Trends Cell Biol. 14:628.
2. Chitu, V. and E.R. Stanley (2006) Curr. Opin. Immunol. 18:39.
3. Fixe, P. and V. Praloran (1997) Eur. Cytokine Netw. 8:125.
4. Ryan, G.R. et al. (2001) Blood 98:74.
5. Makrigiannakis, A. et al. (2006) Trends Endocrinol. Metab. 17:178.
6. Nandi, S. et al. (2006) Blood 107:786.
7. Rettenmier, C.W. and M.F. Roussel (1988) Mol. Cell Biol. 8:5026.
8. Suzu, S. et al. (1992) J. Biol. Chem. 267:16812.
9. Manos, M.M. (1988) Mol. Cell. Biol. 8:5035.
10. Koths, K. (1997) Mol. Reprod. Dev. 46:31.
11. Jang, M-H. et al. (2006) J. Immunol. 177:4055.
12. Kawasaki, E.S. et al. (1985) Science 230: 291.
13. Wong, G.G. et al. (1987) Science 235:1504.

Bioinformatics

• Uniprot:
  • NP_757350.2()