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 2-8 ng/mL.
Source
E. coli-derived feline GM-CSF protein Ala18-Lys144 (Met36Ile, Thr56Ala & Lys126Asn), with an N-terminal Met
>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
Bioactivity
Theoretical MW
14.6 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.
Publications
Read Publications using 987-FL/CF in the following applications:
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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Feline GM-CSF Protein, CF
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 - 10). Mature feline GM-CSF shares 52% - 56% amino acid sequence identity with mouse and rat GM-CSF and 67% - 72% canine, human, and porcine 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 (11, 12). In addition, GM-CSF binds a naturally occurring soluble form of GM-CSF R alpha (13). Feline and human GM-CSF show cross-species activity (14, 15).
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.
Dunham, S.P. and J. Bruce (2004) Gene 332:97.
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.
Sprague, W.S. et al. (2005) J. Comp. Pathol. 133:136.
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