Recombinant Cynomolgus Monkey GM-CSF R alpha His Protein, CF Summary
| Details of Functionality |
Measured by its ability to inhibit GM-CSF-dependent proliferation of TF‑1 human erythroleukemic cells. The ED 50 for this effect is 1.0-5.0 μg/mL in the presence of 40 pg/mLRecombinant Human GM-CSF
(Catalog #
215-GM). |
| Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey GM-CSF R alpha protein Leu20-Arg313, with a C-terminal 6-His tag |
| Accession # |
|
| N-terminal Sequence |
Leu20 |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
34 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 |
59-67 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. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions |
Reconstitute at 500 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 Cynomolgus Monkey GM-CSF R alpha His Protein, CF
Background
Granulocyte macrophage
colony stimulating factor receptor alpha (GM-CSF R alpha ), also known as CD116, is a
component of the receptor complex that mediates cellular responses to GM-CSF.
GM-CSF promotes the differentiation and mobilization of granulocyte-macrophage,
erythroid, megakaryocyte, and eosinophil progenitors. It enhances the
activation of myeloid cell effector functions and plays a role in the
development of Th1 biased immune responses, allergic inflammation, and
autoimmunity (1-4). Mature cynomolgus monkey GM-CSF R alpha is an 80 kDa type I
transmembrane glycoprotein that consists of an extracellular domain (ECD) with
two fibronectin type III domains and a juxtamembrane WSXWS motif, a
transmembrane segment and a cytoplasmic domain (5). Within the ECD, cynomolgus
monkey GM-CSF R alpha shares approximately 90% and 84% amino acid sequence identity with human
and rheus monkey GM-CSF R alpha , respectively. Alternate splicing of GM-CSF R alpha
generates several additional isoforms that lack the cytoplasmic and/or
transmembrane regions. Soluble forms of the receptor retain the ability to bind
GM-CSF (6, 7). GM-CSF R alpha is expressed on hematopoietic stem cells, progenitor
and differentiated cells in the myeloid lineage, vascular endothelial cells,
placenta, and non-hematopoietic solid tumor cells (8). GM-CSF R alpha associates
with the common beta chain/CD131 ( beta c), a 135 kDa transmembrane
protein that is also the signal transducing component of the receptors for IL-3
and IL-5 (9, 10). Association with beta c converts GM-CSF R alpha from a low
affinity to a high affinity receptor for GM-CSF (9-11). The shared usage of beta c
underlies the synergism between GM-CSF, IL-3, and IL-5 in their effects on
myeloid cell differentiation and activation (1, 2).
- Martinez-Moczygemba, M. and D.P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
- Fleetwood, A.J. et al. (2005) Crit. Rev. Immunol. 25:405.
- Eksioglu, E.A. et al. (2007) Exp. Hematol. 35:1163.
- Cao, Y. (2007) J. Clin. Invest. 117:2362.
- Gearing, D.P. et al. (1989) EMBO J. 8:3667.
- Pelley, J.L. et al. (2007) Exp. Hematol. 35:1483.
- Raines, M.A. et al. (1991) Proc. Natl. Acad. Sci. 88:8203.
- Chiba, S. et al. (1990) Cell Regul. 1:327.
- Kitamura, T. et al. (1991) Proc. Natl. Acad. Sci. 88:5082.
- Hayashida, K. et al. (1990) Proc. Natl. Acad. Sci. 87:9655.
- Hoang, T. et al. (1993) J. Biol. Chem. 268:11881.
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