Recombinant Human GM-CSF GMP Protein, CF

Animal-Free.
  
  • Purity
    >97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 6-30 pg/mL.
    The specific activity of recombinant human GM-CSF is approximately 1.5 x 104 IU/μg, which is calibrated against human GM-CSF WHO International Standard (NIBSC code: 88/646).
  • Source
    E. coli-derived Ala18-Glu144 Produced using non-animal reagents in an animal-free laboratory.
    Manufactured and tested under cGMP guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis
    Ala-Pro-Ala-Arg-Ser-Pro-Ser-Pro-Ser-Thr
  • Predicted Molecular Mass
    14.5 kDa
  • SDS-PAGE
    14 kDa, reducing conditions
215-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100-200 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 GM-CSF (Catalog # 215-GMP) stimulates pro­liferation of TF‑1 human erythroleukemic cell line. The ED50 is 6-30 pg/mL.
1 μg/lane of GMP-grade Recombinant Human GM-CSF (Catalog # 215-GMP) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 14 kDa.
Mass Spectrometry
MALDI-TOF analysis of GMP-grade Recombinant Human GM-CSF (Catalog # 215-GMP). The major peak corresponds to the calculated molecular mass, 14478 Da. The minor peak at 14673 Da is a matrix-associated artifact of the MALDI-TOF.
Background: GM-CSF
GM‑CSF was initially characterized as a factor that can support the in vitro colony formation of granulocyte‑macrophage progenitors. It is also a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. GM‑CSF is produced by a number of different cell types (including T cells, B cells, macrophages, mast cells, endothelial cells, fibroblasts, and adipocytes) in response to cytokine or inflammatory stimuli. On mature hematopoietic cells, GM‑CSF is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages, and eosinophils (1, 2). GM‑CSF promotes a Th1 biased immune response, angiogenesis, allergic inflammation, and the development of autoimmunity (3‑5). It shows clinical effectiveness in ameliorating chemotherapy‑induced neutropenia, and GM‑CSF transfected tumor cells are utilized as cancer vaccines (6, 7). The 22 kDa glycosylated GM‑CSF, similar to IL‑3 and IL‑5, is a cytokine with a core of four bundled
alpha -helices (8‑12). Mature human GM‑CSF shares 63%‑70% amino acid sequence identity with canine, feline, porcine, and rat GM‑CSF and 54% with mouse GM‑CSF. GM‑CSF exerts its biological effects through a heterodimeric receptor complex composed of GM‑CSF R alpha /CD116 and the signal transducing common beta  chain (CD131) which is also a component of the high‑affinity receptors for IL‑3 and IL‑5 (13, 14). In addition, GM‑CSF binds a naturally occurring soluble form of GM‑CSF R alpha (15). Human GM‑CSF is active on canine and feline cells but not on murine cells (16‑18).
  • References:
    1. Martinez-Moczygemba, M. and D.P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
    2. Barreda, D.R. et al. (2004) Dev. Comp. Immunol. 28:509.
    3. Eksioglu, E.A. et al. (2007) Exp. Hematol. 35:1163.
    4. Cao, Y. (2007) J. Clin. Invest. 117:2362.
    5. Fleetwood, A.J. et al. (2005) Crit. Rev. Immunol. 25:405.
    6. Heuser, M. et al. (2007) Semin. Hematol. 44:148.
    7. Hege, K.M. et al. (2006) Int. Rev. Immunol. 25:321.
    8. Kaushansky, K. et al. (1992) Biochemistry 31:1881.
    9. Diederichs, K. et al. (1991) Science 254:1779. 
    10. Cantrell, M.A. et al. (1985) Proc. Natl. Acad. Sci. 82:6250.
    11. Lee, F. et al. (1985) Proc. Natl. Acad. Sci. 82:4360.
    12. Wong, G.G. et al. (1985) Science 228:810.
    13. Onetto-Pothier, N. et al. (1990) Blood 75:59.
    14. Hayashida, K. et al. (1990) Proc. Natl. Acad. Sci. 87:9655.
    15. Pelley, J.L. et al. (2007) Exp. Hematol. 35:1483.
    16. Hogge, G.S. et al. (1990) Cancer Gene Ther. 6:26.
    17. Sprague, W.S. et al. (2005) J. Comp. Pathol. 133:136.
    18. Shanafelt, A.B. et al. (1991) J. Biol. Chem. 266:13804.
  • Long Name:
    Granulocyte Macrophage Growth Factor
  • Entrez Gene IDs:
    1437 (Human); 12981 (Mouse); 116630 (Rat); 397208 (Porcine); 403923 (Canine); 493805 (Feline)
  • Alternate Names:
    colony stimulating factor 2 (granulocyte-macrophage); Colony-stimulating factor; CSF; CSF2; GMCSF; GM-CSF; GMCSFgranulocyte-macrophage colony-stimulating factor; granulocyte-macrophage colony stimulating factor; MGC131935; MGC138897; molgramostin; sargramostim

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