Recombinant Human GM-CSF (CHO-expressed) Protein Summary
| Additional Information |
Analyzed by SEC-MALS |
| 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 ED 50 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 |
|
| 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 in the following applications:
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Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
| Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
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
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).
- Martinez-Moczygemba, M. and D.P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
- Barreda, D.R. et al. (2004) Dev. Comp. Immunol. 28:509.
- Eksioglu, E.A. et al. (2007) Exp. Hematol. 35:1163.
- Cao, Y. (2007) J. Clin. Invest. 117:2362.
- Fleetwood, A.J. et al. (2005) Crit. Rev. Immunol. 25:405.
- Heuser, M. et al. (2007) Semin. Hematol. 44:148.
- Hege, K.M. et al. (2006) Int. Rev. Immunol. 25:321.
- Kaushansky, K. et al. (1992) Biochemistry 31:1881.
- Diederichs, K. et al. (1991) Science 254:1779.
- Cantrell, M.A. et al. (1985) Proc. Natl. Acad. Sci. 82:6250.
- Lee, F. et al. (1985) Proc. Natl. Acad. Sci. 82:4360.
- Wong, G.G. et al. (1985) Science 228:810.
- Onetto-Pothier, N. et al. (1990) Blood 75:59.
- Hayashida, K. et al. (1990) Proc. Natl. Acad. Sci. 87:9655.
- Pelley, J.L. et al. (2007) Exp. Hematol. 35:1483.
- Hogge, G.S. et al. (1990) Cancer Gene Ther. 6:26.
- Sprague, W.S. et al. (2005) J. Comp. Pathol. 133:136.
- Shanafelt, A.B. et al. (1991) J. Biol. Chem. 266:13804.
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