Human GM-CSF
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| Cat-Nr. | 400-011 |
| Size | 20 µg |
| Price | 350 € |
| Source | Insect cells |
| Label | His-Tag |
| Formulation | lyophilized |
| Purity Confirmation | > 98% by SDS-PAGE |
| Length [aa] | 135 |
| Molecular Weight | ~15-18 kDa |
| N Terminal Sequence | APARSPSPST |
| Endotoxin Levels | < 0.1 ng per µg of GM-CSF |
| Biological Activity | Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells [Kitamura T et al, J Cell Physiol, 1989]. The ED50 for this effect is typically <0.1 ng/ml corresponding to a specific activity of ≥1 x 107 units/mg. |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The lyophilized rh GM-CSF is soluble in water and most aqueous buffers and can be reconstituted in water to a concentration of 0.1 mg/ml. This solution can be diluted into other buffered solutions or stored at -20°C for future use. |
| Stability and Storage | The lyophilized powder although stable at room temperature for 3 weeks, is best stored desiccated at -20°C. Reconstituted GM-CSF should be stored in working aliquots at -20°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). |
| Synonyms | CSF2; GMCSF |
| Description | Granulocyte Macrophage Colony Stimulating Factor (GM-CSF), a 14,6 kDa protein consisting of 127 amino acid residues (Ala18-Glu144) and fused to a C-terminal His-tag (6x His), is a potent species specific stimulator of bone marrow cells and several other cell types. GM-CSF was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It is produced by a number of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cells and fibroblasts) in response to cytokine or immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, GM-CSF is also a growth factor for erythroid, megakaryocyte and eosinophil progenitors. On mature hematopoietic cells, GM-CSF is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages and eosinophils. GM-CSF has also been reported to have a functional role on non-hematopoietic cells. It can induce human endothelial cells to migrate and proliferate. Additionally, GM-CSF can also stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. GM-CSF is species specific and human GM-CSF has no biological effects on mouse cells. GM-CSF exerts its biological effects through binding to specific cell surface receptors. The high affinity receptors required for human GM-CSF signal transduction have been shown to be heterodimers consisting of a GM-CSF-specific α chain and a common β chain that is shared by the high-affinity receptors for IL-3 and IL-5. |
| Protein Sequence | APARSPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEPVQETRHHHHHH |
| Uniprot ID | P04141 |
| Protein RefSeq | NP_000749 |
| mRNA RefSeq | NM_000758 |
Figures
SDS-PAGE analysis of recombinant human GM-CSF. Sample was loaded in 15% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue. There are different glycosylation forms visible.
Dose-dependent stimulation of cell proliferation in TF-1 cells by recombinant human GM-CSF. Values are the means (±SD) of triplicate determinations and expressed as percentage of control.
Reference
- Endothelial Cell Activation by SARS-CoV-2 Spike S1 Protein: A Crosstalk between Endothelium and Innate Immune Cells. B. M. Rotoli et al., Biomedicines. 2021 Sep; 9(9): 1220.
- Human Neutrophil Peptide-1 (HNP-1): A New Anti-Leishmanial Drug Candidate. S. Dabirian et al., PLoS Negl Trop Dis. 2013 Oct; 7(10): e2491.
- Inflammatory Macrophages Induce Nrf2 Transcription Factor-dependent Proteasome Activity in Colonic NCM460 Cells and Thereby Confer Anti-apoptotic Protection. S. Sebens et al., J Biol Chem. 2011 Nov 25; 286(47): 40911–40921.
- In Lysinuric Protein Intolerance system y+L activity is defective in monocytes and in GM-CSF-differentiated macrophages. A. Barilli et al., Orphanet J Rare Dis. 2010; 5: 32.
- Hantavirus Infection of Dendritic Cells. M. J. Raftery et al., J Virol. 2002 Nov; 76(21): 10724–10733.
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