Recombinant Human GM-CSF (CHO) Biotinylated Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated
Recombinant Human GM-CSF (Catalog # BT7954) binds Recombinant Human GM-CSF R alpha (Catalog #
706-GR) in the presence of Recombinant Human
Common beta Chain His-tag (Catalog #
9960-CB) with an ED 50 of 20.0-240 ng/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human GM-CSF protein Ala18-Glu144 |
| Accession # |
|
| N-terminal Sequence |
Ala18 |
| Structure / Form |
Biotinylated via amines |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note |
<0.10 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 |
14-28 kDa, under reducing conditions. |
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 with Trehalose. |
| Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions |
Reconstitute at 250 μg/mL in water. |
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) Biotinylated Protein, CF
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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