E24PCA164

Cynomolgus / Rhesus Macaqu CSF2 / GM-CSF, hFc Tag

1860.42 €

E24PCA163

Cynomolgus / Rhesus Macaqu CSF2 / GM-CSF, His Tag

1860.42 €

E21-C79

GM-CSF/CSF2

Recombinant Human Granulocyte-Macrophage Colony-Stimulating Factor is produced by our Mammalian expression system and the target gene encoding Ala18-Glu144 is expressed with a 6His tag at the C-terminus.

492.38 €

Z200075

Recombinant Mouse GM-CSF (CSF2)

GM-CSF is a monomeric cytokine with two glycosylation sites that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. CSF2 is secreted together with other factors by T cells and macrophages following cell activation by antigens or mitogens. The signalling ‘GM-CSF:receptor’ complex is a dodecamer of two hexamers of two alpha, two beta, and two ligand subunits. While non-glycosylated and glycosylated GM-CSF show similar activities in vitro, fully glycosylated GM-CSF is biologically more active in vivo. Recombinant Mouse CSF2 is a non-glycosylated, monomeric protein.

405.01 €

Z200077

Recombinant Mouse GM-CSF (CSF2)

GM-CSF is a monomeric cytokine with two glycosylation sites that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. CSF2 is secreted together with other factors by T cells and macrophages following cell activation by antigens or mitogens. The signalling ‘GM-CSF:receptor’ complex is a dodecamer of two hexamers of two alpha, two beta, and two ligand subunits. While non-glycosylated and glycosylated GM-CSF show similar activities in vitro, fully glycosylated GM-CSF is biologically more active in vivo. Recombinant Mouse CSF2 is a non-glycosylated, monomeric protein.

1404.91 €

Z200079

Recombinant Mouse GM-CSF (CSF2)

GM-CSF is a monomeric protein of 127 amino acids with two glycosylation sites. The protein is synthesized as a precursor of 144 amino acids, which included a hydrophobic secretory signal sequence at the aminoterminal end. The sugar moiety is not required for the full spectrum of biological activities. Non-glycosylated and glycosylated GM-CSF show the same activities in vitro. Fully glycosylated GM-CSF is biologically more active in vivo than the non- glycosylated protein. This protein is secreted together with other factors by T cells and macrophages following cell activation by antigens or mitogens. Approximately 90% of the secreted colony stimulating activities are due to GM-CSF.

6707.41 €