Recombinant Mouse GM-CSF Protein

Name: Recombinant Mouse GM-CSF Protein
Brand: Beta LifeScience
SKU: BL-1708NP
Availability: InStock

BL-1708NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Colony-stimulating factors and receptors (csfs), Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Granulocyte-Macrophage Colony-Stimulating Factor is produced by our E.coli expression system and the target gene encoding Ala18-Lys141 is expressed.
Accession	P01587
Synonym	Granulocyte-macrophage colony-stimulating factor; Csf2; GM-CSF; Colony-stimulating factor; Csfgm
Gene Background	Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factorthat can support the in vitro colony formation of granulocyte-macrophage progenitors. It is produced by anumber of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cellsand fibroblasts) in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophageprogenitors, GM-CSF is also a growth factor for erythroid, megakaryocyte and eosinophil progenitors. Onmature hematopoietic, monocytes/ macrophages and eosinophils. GM-CSF has a functional role on nonhematopoitic cells. It can induce human endothelial cells to migrate and proliferate. Additionally, GM-CSF canalso stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma andadenocarcinoma cell lines.
Molecular Mass	14.2 KDa
Apmol Mass	15 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 1mM EDTA, pH 8.0.
Endotoxin	Less than 0.001 ng/µg (0.01 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Biologically active. Please contact us to obtain bioactivity data.
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Subcellular Location	Secreted.
Protein Families	GM-CSF family
Database References	KEGG: mmu:12981 STRING: 10090.ENSMUSP00000019060 UniGene: Mm.4922

Gene Functions References

Data show that the microbiota enhances respiratory defenses via granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling, which stimulates pathogen killing and clearance by alveolar macrophages PMID: 29142211
The data indicate that GM-CSF drives chronic tissue damage and disability in experimental autoimmune encephalomyelitis via pleiotropic pathways, but it is dispensable during early lesion formation and the onset of neurologic deficits. PMID: 29288202
the release of IL-33 and GM-CSF from epithelial cells induces the activation of p65 and the p38-MK2/3 signaling module in Dendritic Cells, resulting in Th2 polarization and, finally, allergic inflammation. PMID: 29288203
results show T cell production of GM-CSF contributes to control of M. tuberculosis infection in the absence of other sources of GM-CSF, that multiple T cell subsets make GM-CSF in the lung over the course of infection and that GM-CSF can act directly on infected macrophages through a pathway requiring PPARgamma to limit bacterial growth PMID: 29066547
In conclusion, our study confirms the pathogenic role of GM-CSF in colitis-associated colorectal cancer development. GM-CSF favors tumor-permissive microenvironment by inducing MDSC generation and recruiting them into colonic tissues. PMID: 28534709
these data demonstrate that GM-CSF levels during radiotherapy can be used as a prognostic biomarker for lung and esophageal cancer PMID: 27835886
this study demonstrates that epithelial-derived GM-CSF is a critical early signal during allergic sensitization to cockroach allergen PMID: 27731325
These impaired macrophage functions in leukemic mice were significantly corrected by IL-3 and GM-CSF treatment indicating the therapeutic benefit of these two cytokines in leukemia. PMID: 28039843
Both IL-6 protein production and transcript levels were downregulated by RA in respiratory tract epithelial cells (LETs) , but upregulated in macrophages (MACs). RA also increased transcript levels of MCP-1, GMCSF, and IL-10 in MACs, but not in LETs. Conversely, when LETs, but not MACs, were exposed to RA PMID: 27940088
T-GM-CSF and -IL-3 significantly, and reciprocally, blunted receptor binding and myeloid progenitor cell proliferation activity of both FL-GM-CSF and -IL-3 in vitro and in vivo PMID: 28344320
Results indicate GM-CSF as both a key contributor to the pathogenesis of MI and a potential therapeutic target. PMID: 28978634
Obesity alters the lung neutrophil infiltration to enhance breast cancer metastasis through IL5 and GM-CSF. PMID: 28737771
GM-CSF is required for the normal balance of leukocyte subsets, including granulocytes, B cells, and naive vs. effector T cells. There was an approximately 3-fold increase in the percentages of granulocytes in Csf2-/- PBMCs. The presence of maximal experimental autoimmune encephalomyelitis in the complete absence of GM-CSF revealed that GM-CSF is not an obligate effector molecule in all forms of EAE. PMID: 27256565
chemerin inhibited nuclear factor-kappaB activation and the expression of granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin-2 (IL-6) by tumor cells and tumor-associated endothelial cell, respectively, via its receptors, and consequently, MDSC induction was impaired, leading to restoration of antitumor T-cell response and decreased tumor angiogenesis. PMID: 28166197
These findings describe a novel role for GM-CSF as an essential initiating cytokine in cardiac inflammation. PMID: 27595596
Data reviewed establish that any damage to brain tissue tends to cause an increase in G-CSF and/or GM-CSF (G(M)-CSF) synthesized by the brain. Glioblastoma cells themselves also synthesize G(M)-CSF. G(M)-CSF synthesized by brain due to damage by a growing tumor and by the tumor itself stimulates bone marrow to shift hematopoiesis toward granulocytic lineages away from lymphocytic lineages. PMID: 28459367
Evi1(+)DA-3 cells modified to express an intracellular form of GM-CSF, acquired growth factor independence and transplantability and caused an overt leukemia in syngeneic hosts, without increasing serum GM-CSF levels. PMID: 25907616
IL-23-induced GM-CSF mediates the pathogenicity of CD4(+) T cells in experimental autoimmune myocarditis. PMID: 26660726
GM-CSF accelerated the G1/S phase transition in EPCs by upregulating the expression of cyclins D1 and E. PMID: 24662605
host RNF13 affects the concentration of GM-CSF in tumor-bearing lungs PMID: 26197965
Sc CW-derived BG stimulated the late and strong expression of Csf2 in a dectin-1-dependent manner, they remain poor inducers of chemokine and cytokine production in murine macrophages. PMID: 26840954
GM-CSF and uPA are required for Porphyromonas gingivalis-induced alveolar bone loss in a mouse periodontitis model. PMID: 25753270
These findings identify GM-CSF as central to the protective immune response that prevents progressive fungal disease PMID: 26755822
regulatory molecule causative of aortic dissection and intramural haematoma PMID: 25923510
Results indicate that granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling controls a pathogenic expression signature in CC chemokine receptors 2 (CCR2+)Ly6C(hi) monocytes. PMID: 26341401
TL1A increases expression of CD25, LFA-1, CD134 and CD154, and induces IL-22 and GM-CSF production from effector CD4 T-cells PMID: 25148371
Mafb-deficient microglia cultured with GM-CSF barely extended their membrane protrusions, probably due to abnormal activation of RhoA, a key regulator of cytoskeletal remodeling. MafB is a negative regulator of GM-CSF signaling in microglia. PMID: 25998393
Csf2-/- mice showed a 30% increase in whole body adiposity, which persisted to adulthood. Adipocytes from Csf2-/- mice were 50% larger by volume and contained higher levels of adipogenesis gene transcripts, indicating enhanced adipocyte differentiation. PMID: 25931125
Renal ischemia reperfusion injury tubular cells expressed elevated GM-0CSF, that supports tubular cells proliferation. PMID: 25388222
GM-CSF is key to the development of experimental osteoarthritis and its associated pain. PMID: 22995428
Loss of encephalitogenic activity of STAT5-deficient autoreactive CD4+ T cells was independent of IFN-gamma or IL-17 production, but was due to the impaired expression of GM-CSF, a crucial mediator of T-cell pathogenicity. PMID: 25412660
These data indicate that GM-CSF plays a role in the inflammatory signaling network that drives neutrophil recruitment in response to Clostridium difficile infection but does not appear to play a role in clearance of the infection. PMID: 25045999
IRF8 represses GM-CSF expression in T cells to affect myeloid cell lineage differentiation. PMID: 25646302
Reprogramming of monocytes by GM-CSF contributes to regulatory immune functions during intestinal inflammation. PMID: 25653427
GM-CSF promotes advanced plaque progression by increasing macrophage apoptosis susceptibility. PMID: 25348165
although iTreg cells maintained the ability to produce IFN-gamma and TNF-alpha in vivo, their ability to produce GM-CSF was selectively degraded upon antigen stimulation under inflammatory conditions. PMID: 25168419
IFN-gamma has a pprotective role in the demyelination of brain through downregulation of IL-17/GM-CSF and induction of neuroprotective factors in the brain by monocytes/microglial cells. PMID: 25339670
Expression of PPAR-gamma in fetal lung monocytes was dependent on the cytokine GM-CSF. Therefore, GM-CSF has a lung-specific role in the perinatal development of alveolar macrophages through the induction of PPAR-gamma in fetal monocytes. PMID: 25263125
These novel findings indicate that the inflammatory mediator, GM-CSF, may have significant protective properties in the chronic sequelae of experimental Traumatic brain injury PMID: 24392832
Airway infections and pollutants increase the susceptibility to develop allergic asthma through a GM-CSF/IL-33/OX40L pathway. PMID: 24551140
Data indicate that neutralization of GM-CSF would be a useful therapeutic strategy for severe connective tissue diseases (CTD)-interstitial lung disease (ILD). PMID: 24951817
Data indicate that lung epithelium-derived GM-CSF is a critical regulator of CD11b+ dendritic cells (DCs)-mediated Th2 cell priming. PMID: 24943219
Bhlhe40 is required positively regulates the production of GM-CSF and negatively regulates the production of IL-10 in T cells. PMID: 24699451
Report IL-18 plus GM-CSF modified tumor cell vaccine can induce significant antitumor effects in Lewis lung carcinoma. PMID: 24475975
Data indicate that in type 1 diabetes monocytes STAT5Ptyr activation is significantly higher and is found bound to CSF2 promoter and PTGS2 enhancer regions. PMID: 24204704
Data indicate that GM-CSF controls IgM production in innate response activator B cells. PMID: 24821911
our findings suggest that over-production of GM-CSF by T cells could be a pathogenic factor in many histiocytic disorders PMID: 24183847
that p52 binds to the promoter of the GM-CSF-encoding gene (Csf2) and cooperates with c-Rel in the transactivation of this target gene. PMID: 24899500
GM-SCF, IL-21 and Rae1 expression, alone or in combination, induces a cellular immune response against H22 tumor cells. PMID: 24350772
Data indicate that GM-CSF knockout mice exhibit a unique mix of M1-M2 macrophage phenotypes inalveolar macrophages. PMID: 24044676

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.