Recombinant Human G-CSF protein

Background

Granulocyte colony stimulating factor (G-CSF) is a pleiotropic cytokine. It is mainly produced by monocytes and macrophages upon activation by endotoxin, TNF-α and IFN-γ. Besides, many other cell types can secreted this protein after LPS, IL-1 or TNF-α activation, which are fibroblasts, endothelial cells, astrocytes and bone marrow stromal cells. Various carcinoma cell lines and myeloblastic leukemia cells can express G-CSF constitutively. G-CSF is cytokine that acts in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. In addition it may function in some adhesion or recognition events at the cell surface. In humans, two distinct cDNA clones for G-CSF, encoding 207 and 204 amino acid (a.a.) precursor proteins, have been isolated. Both proteins have a 30 a.a. signal peptide and have identical amino acid sequences except for a three a.a. insertion (deletion) at the 35th a.a. residue from the N-terminus of the mature protein. Human G-CSF is 73 % identical at the amino acid level to Mouse G-CSF and the two proteins show species cross-reactivity.

Expression system

Escherichia coli.

Purity

> 98 % by SDS-PAGE and HPLC analyses.

Molecular weight

Approximately 18.7 kDa, a single non-glycosylated polypeptide chain containing 174 amino acids.

Endotoxin

Less than 1 EU/μg of rHuG-CSF as determined by LAL method.

Form

Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10mM sodium acetate buffer, containing 5 % trehalose, pH 4.0.

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