Recombinant Human M-CSF GMP Protein, CF

Animal-Free.
  
  • Purity
    >97%, by SDS-PAGE with silver staining, under reducing conditions.
  • Endotoxin Level
    <0.01 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a cell proliferation assay using M‑NFS‑60 mouse myelogenous leukemia lymphoblast cells. Nakoinz, I. et al. (1990) J. Immunol. 145:860. The ED50 for this effect is 0.5-1.5 ng/mL.

    The specific activity of Recombinant Human M-CSF is approximately 1.68 x 105 IU/μg, which is calibrated against recombinant human
    M-CSF WHO International Standard (NIBSC code: 89/512).
  • Source
    E. coli-derived Glu33-Ser190, with an N-terminal Met Produced using non-animal reagents in an animal-free laboratory.
    Manufactured and tested under cGMP guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis
    Met-Glu-Glu-Val-Ser-Glu-Try-(Cys)-Ser-His
  • Structure / Form
    Disulfide-linked homodimer
  • Predicted Molecular Mass
    18.5 kDa (monomer)
  • SDS-PAGE
    37 kDa, non-reducing conditions
216-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 50-500 μg/mL in PBS.
Shipping 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.
  • A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Data Images
GMP-grade Recombinant Human M-CSF (Catalog # 216-GMP) stimulates cell proliferation in the M‑NFS‑60 mouse myelogenous leukemia lymphoblast cell line in a dose-dependent manner. The ED50 for this effect is 0.5-1.5 ng/mL.
1 μg/lane of GMP-grade Recombinant Human M-CSF (Catalog # 216-GMP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 18 kDa and 32 kDa, respectively.
Mass Spectrometry
ESI analysis of GMP-grade Recombinant Human M-CSF (Catalog # 216-GMP). The peak at 37056 Da corresponds to the measured molecular weight of the intact dimer. The calculated mass for the monomer is 18535 Da.
Background: M-CSF
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.
  • References:
    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.
  • Long Name:
    Macrophage Colony Stimulating Factor
  • Entrez Gene IDs:
    1435 (Human); 12977 (Mouse)
  • Alternate Names:
    colony stimulating factor 1 (macrophage); CSF1; CSF-1; Lanimostim; macrophage colony stimulating factor; macrophage colony-stimulating factor 1; MCSF; M-CSF; MCSFlanimostim; MGC31930

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