Recombinant Human NGF

Description
Nerve growth factor (NGF) is important for the development and maintenance of the sympathetic and sensory nervous systems. NGF was identified as a large complex consisting of three non-covalently linked subunits, α, β, and γ, among which, the β subunit, called β-NGF, was demonstrated to exhibits the growth stimulating activity of NGF. β-NGF is a target-derived secreted homodimeric protein of two 120-amino acid mature polypeptides after proteolytic removal of the signal and pro peptide. NGF acts via at least two receptors on the surface of cells, TrkA and p75 receptors to regulate neuronal survival, promote neurite outgrowth, and up-regulate certain neuronal functions such as mediation of pain and inflammation. In addition to its neurotropic activities, studies indicated that NGF may also have an important role in the regulation of the immune system.

Full Name
Nerve Growth Factor (beta polypeptide)

Source
E. coli

Species
Human

Molecule Weight
The mature recombinant human β-NGF consists of 120 amino acids and has a predicted molecular mass of 13.5 kDa. β-NGF exists as a non-disulfide linked homodimer in solution.

Purity
> 95 % as determined by SDS-PAGE

Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method

Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is typically 0.2-2 ng/ml.

Storage
-80 °C, avoid repeated freeze-thaw cycles.

Storage Buffer
PBS