Detects mouse M‑CSF in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 5% cross-reactivity with recombinant human (rh) M‑CSF is observed. Neutralizes the biological activity of recombinant mouse M-CSF and will also neutralize the biological activity of recombinant human M-CSF at a 100 fold higher IgG concentration.
Polyclonal Goat IgG
Protein A or G purified
E. coli-derived recombinant mouse M-CSF Lys33-Glu262 Accession # Q3U4F9
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize M‑CSF-induced proliferation in the M‑NFS‑60 mouse myelogenous leukemia lymphoblast cell line. Halenbeck, R. et al. (1989) Biotechnology 7:710. The Neutralization Dose (ND50) is typically 0.2-0.6 µg/mL in the presence of 10 ng/mL Recombinant Mouse M‑CSF.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Cell Proliferation Induced by M‑CSF and Neutralization by Mouse M‑CSF Antibody.
Recombinant Mouse M‑CSF (Catalog # 416-ML) stimulates proliferation in the M‑NFS‑60 mouse myelogenous leukemia lymphoblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Mouse M‑CSF (10 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Mouse M‑CSF Polyclonal Antibody (Catalog # AB-416-NA). The ND50 is typically 0.2‑0.6 µg/mL.
Preparation and Storage
Reconstitute at 1 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 mouse M-CSF transcripts encode a 520 amino acid (aa) type I transmembrane (TM) protein with a 462 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 229 aa of mature mouse M-CSF shares 87%, 83%, 82% and 81% aa identity with corresponding regions of rat, dog, cow and human M-CSF, respectively (12, 13). Human M‑CSF is active in the mouse, but mouse M-CSF is reported to be species-specific.
Pixley, F.J. and E.R. Stanley (2004) Trends Cell Biol. 14:628.
Chitu, V. and E.R. Stanley (2006) Curr. Opin. Immunol. 18:39.
Fixe, P. and V. Praloran (1997) Eur. Cytokine Netw. 8:125.
Ryan, G.R. et al. (2001) Blood 98:74.
Makrigiannakis, A. et al. (2006) Trends Endocrinol. Metab. 17:178.
Nandi, S. et al. (2006) Blood 107:786.
Rettenmier, C.W. and M.F. Roussel (1988) Mol. Cell Biol. 8:5026.
Suzu, S. et al. (1992) J. Biol. Chem. 267:16812.
Manos, M.M. (1988) Mol. Cell. Biol. 8:5035.
Koths, K. (1997) Mol. Reprod. Dev. 46:31.
Jang, M-H. et al. (2006) J. Immunol. 177:4055.
DeLamarter, J.F. et al. (1987) Nucleic Acids Res. 15:2389.
Ladner, M.B. et al. (1988) Proc. Natl. Acad. Sci. USA 85:6706.
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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