mouse NGF 2.5S (>95%)

Non Antibodies

Proteins

Israel

Storage as Solution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. - Storage before Reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. - Storage after Reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.

Lyophilized

Nerve Growth Factor 2.5S - Native Mouse Nerve Growth Factor

Native Mouse Nerve Growth Factor

12352202

EC50 = 0.7 nM

Centrifuge the vial before adding solvent (10, 000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. Repeat freeze-thawing may result in loss of activity.

The neurotrophins ("neuro" means nerve and "trophe" means nutrient) are a family of soluble, basic growth factors which regulate neuronal development, maintenance, survival and death in the CNS and PNS.1NGF, the first member of the family to be discovered, was originally purified as a factor able to support survival of sympathetic and sensory spinal neurons in culture.2 It is synthesized and secreted by sympathetic and sensory target organs and provides trophic support to neurons as they reach their final target.3Neurotrophin secretion increases in the nervous system following injury. Schwann cells, fibroblasts, and activated mast cells normally synthesize NGF constitutively, however direct trauma and induction of cytokines combine to increase neurotrophin production in these cells after injury.4NGF is purified in three forms: the 7S, 2.5S and β. The 7S (130 kDa) form occurs naturally in mouse submaxillary glands, and is a multimeric protein composed of two α, one β and two γ subunits. The name is derived from its sedimentation co-efficient, 7S.The biologically active subunit is the β, which is a 26 kDa dimer composed of two identical 120 amino acid chains held together by hydrophobic interactions.5 The 2.5S form is 9 amino acids shorter than the β form because of proteolysis that occurs during the purification process.6 The structural hallmark of all the neurotrophins is the characteristic arrangement of the disulfide bridges known as the cysteine knot, which has been found in other growth factors such as Platelet-derived growth factor.7 There is a 95.8% homology between the rat and mouse forms, and a 85% homology between the human and mouse.NGF has been shown to regulate neuronal survival, development, function and plasticity.8 Recently, involvement of NGF in processes not involving neuronal cells has been shown, such as asthma, 9 psoriasis10 and wound healing.11 The biological effects of NGF are mediated by two receptors: TrkA, which is specific for NGF, and p75NTR, which binds all the neurotrophins.12