Recombinant Mouse G-CSF

Cat # Size Price Quantity
67100120 μg$320
671002200 μg$890

Product Details


ApplicationBioassay
FormatLyophilized from sterile PBS, pH 7.4.
Expression HostHEK293
Target NameG-CSF, Granulocyte-Colony Stimulating Factor, CSF3
SpeciesMouse
accession numberNP_034101.1
SourcesA DNA sequence encoding the mouse CSF3 (NP_034101.1) (Met1-Ala208) was expressed and purified.
Molecular WeightThe recombinant mouse CSF3 consists of 178 amino acids and predicts a molecular mass of 19 KDa. The molecular weight of this protein is around 19.2 KDa verified by SEC-MALS(Routinely tested).
Affinity TagNone
Purity≥95% as determined by SDS-PAGE.
Regulatory StatusRUO
Endotoxin level< 0.1 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information


Mouse granulocyte colony-stimulating factor (G-CSF), also known as colony-stimulating factor 3 (CSF3), is a secreted cytokine that regulates the production, differentiation, survival, and mobilization of neutrophils. It is an essential component of innate immunity, helping maintain neutrophil levels during normal hematopoiesis and increasing neutrophil production during infection or inflammation. G-CSF also promotes the functional activation of mature neutrophils, supporting their migration to sites of infection and their antimicrobial activities.



Mouse G-CSF is a glycoprotein belonging to the class I hematopoietic cytokine family. It is synthesized as a precursor protein and processed into a mature, secreted polypeptide of approximately 178 amino acids. Its structure consists of a characteristic four-helix bundle stabilized by intramolecular disulfide bonds. Glycosylation may influence its stability and biochemical properties. G-CSF functions as a soluble ligand that binds to the granulocyte colony-stimulating factor receptor (G-CSFR), also known as CSF3R or CD114, which is expressed primarily on neutrophil precursors and mature neutrophils.



Binding of G-CSF to G-CSFR induces receptor dimerization or rearrangement, activating intracellular signaling pathways, including JAK/STAT, MAPK, and PI3K/AKT. These pathways regulate myeloid cell proliferation, differentiation, survival, and mobilization from the bone marrow. G-CSF signaling is tightly controlled because excessive activity can contribute to abnormal neutrophil expansion and inflammatory responses.



Dysregulation of G-CSF production or signaling is associated with neutropenia, excessive neutrophilic inflammation, and certain malignancies. In some cancers, tumor-derived G-CSF can promote neutrophil expansion and contribute to an immunosuppressive tumor microenvironment. Therapeutically, recombinant G-CSF, including filgrastim and related agents, is widely used in humans to prevent or treat chemotherapy-induced neutropenia and to mobilize hematopoietic stem cells for transplantation. Mouse G-CSF is particularly valuable in preclinical studies investigating granulopoiesis, infection, inflammation, bone marrow recovery, and the development of cytokine-based therapies.

Data Sheets


Recombinant Mouse G-CSF TDS

Frequently Asked Questions


What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.

What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.

How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.

Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.

Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

Have a product or application question? Consult our FAQs or contact us.