Recombinant M-CSF, Human
Catalogue Numbers: BK0127-10, BK0127-100
Sizes: 10μg, 100μg
Source: Escherichia coli
Molecular Weight: 28 kDa, observed by non-reducing SDS-PAGE.
Purity: > 95% as analyzed by non-reducing SDS-PAGE.
Biological Activity: ED50 of 1 - 3 ng/ml, measured by cell proliferation assay of M-NFS-60, corresponding to a specific activity of 3.3 x 10ˆ5-1 x 10ˆ6 units/mg.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized after extensive dialysis against 50 mM Tris-HCl, pH 8.0.
AA Sequence: MEEVSEYCS HMIGSGHLQS LQRLIDSQME TSCQITFEFV DQEQLKDPVC YLKKAFLLVQ DIMEDTMRFR DNTPNAIAIV QLQELSLRLK SCFTKDYEEH DKACVRTFYE TPLQLLEKVK NVFNETKNLL DKDWNIFSKN CNNSFAECSS QGHERQSEGS
Endotoxin: <1 EU/μg, determined by LAL method.
Reconstitution: Reconstituted in ddH2O or PBS or Tris-HCl, pH 8.0 at 100 μg/ml.
Storage: Lyophilized recombinant human Macrophage Colony-Stimulating Factor 1 (rhM-CSF) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhM-CSF should be stable up to 2 weeks at 4°C or up to 3 months at -20°C.
Usage: This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.
Description: Macrophage Colony-Stimulating Factor 1 (M-CSF), involved especially in monocytopoiesis,[1]is a hematopoietic growth factor. In mammals, it exits three isoforms, which invariably share an N-terminal 32-aa signal peptide, a 149-residue growth factor domain, a 21-residue transmembrane region and a 37-aa cytoplasmictail[2]. The biological activity of human M-CSF is maintained within the 149-aa growth factor domain[3], and it is only active in the disulfide-linked dimeric form[4], which is bonded at Cys63.Recombinant human Macrophage Colony-Stimulating Factor 1 (rhM-CSF) produced in E.coli is a disulfide-linked homodimer containing two non-glycosylated polypeptide chains of 159 amino acids each. A fully biologically active molecule, rhM-CSF has a molecular mass of 28 kDaanalyzed by non-reducing SDS-PAGE and is obtained by proprietary refolding and chromatographic techniques at GenScript.