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Recombinant Human GM-CSF (CHO-expressed) Protein, CF

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Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is 6-30 pg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human GM-CSF (CHO-expressed) Protein, CF Summary

Details of Functionality
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.
Source
Chinese Hamster Ovary cell line, CHO-derived human GM-CSF protein
Ala18-Glu144
Accession #
N-terminal Sequence
Ala18
Protein/Peptide Type
Recombinant Proteins
Gene
CSF2
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
14.5 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
20-35 kDa, reducing conditions
Publications
Read Publications using
7954-GM/CF in the following applications:

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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 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 GM-CSF (CHO-expressed) Protein, CF

  • colony stimulating factor 2 (granulocyte-macrophage)
  • Colony-stimulating factor
  • CSF
  • CSF2
  • CSF-2
  • GMCSF
  • GM-CSF
  • GMCSFgranulocyte-macrophage colony-stimulating factor
  • granulocyte-macrophage colony stimulating factor
  • MGC131935
  • MGC138897
  • Molgramostim
  • molgramostin
  • Sargramostim

Background

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).
  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.

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Bioinformatics

Gene Symbol CSF2
Uniprot