|Product Name||Cat #||Size|
|AN-240||1 x 0.2 ml|
Anti-p75NTR (extracellular) Antibody
|ANT-007||1 x 0.2 ml|
Anti-p75NTR (extracellular)-ATTO-488 Antibody
|ANT-007-AG||1 x 50 µl|
Anti-TrkA (extracellular) Antibody
|ANT-018||1 x 0.2 ml|
Anti-TrkA (extracellular)-ATTO-633 Antibody
|ANT-018-FR||1 x 50 µl|
Mouse NGF/proNGF Neutralizing Antibody
|ALM-006||1 x 0.25 mg|
|G-191||1 x 25 mg|
|N-245||1 x 25 µg|
|K-150||1 x 0.1 mg|
- Lyophilized Powder Lyophilized Powder
This product is freeze dried. All water molecules have been removed.
- Antigen Incl. Control Antigen Included
This antibody is shipped with its antigen FREE of charge!
- Fluorescent Label ATTO
This product is "conjugated" to a fluorescent dye.
- Bioassay Tested Bioassay Tested
This antibody has undergone quality control and has been approved by our professional team.
- QC Tested QC Tested
The activity of this product has been verified and approved by our professional team.
- Shipped at Room Temp. Shipped at Room Temp.
This lyophilized product is shipped at room temperature. Please see its certificate of analysis for further storage instructions.
- Live Cell Imaging Live Cell Imaging
This product has been tested in living cells.
- Immuno-Colocalization Immuno-Colocalization
This product is ideal for immuno-colocalization experiments. Secondary antibodies are not needed for conjugated antibodies!
- 100% Net Peptide 100% Net Peptide
This vial contains 100% net peptide content.
- Sterile & Endotoxin Free Sterile & Endotoxin Free
0.1 EU per 1 µg of the protein by the LAL method & lyophilized from a 0.2 µm filtered solution.
Alomone Labs is pleased to offer the Human NGF Deluxe Research Pack (#ESD-650). The Research Pack contains all you need for human NGF research: Antibodies to NGF and its receptors, recombinant NGF and specific TrkA receptor inhibitors all in one economical package!
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 the PNS.1 NGF, 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.3 Neurotrophin secretion also increases in the nervous system following injury. Schwann cells, fibroblasts, and activated mast cells normally synthesize NGF constitutively, however direct trauma and induced cytokines combine to increase neurotrophin production in these cells after injury.4
NGF 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 PDGF.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
- Roux, P. and Barker P. A. (2002) Prog. Neurobiol. 67, 203.
- Levi-Montalcini, R. (1966) Harvey Lect. 60, 217.
- Farinas, I. et al. (1998) Neuron 21, 325.
- Levi-Montalcini, R. et al. (1996) Trends Neurosci. 19, 514.
- Bradshaw, R.A. (1978) Ann. Rev. Biochem 47, 191.
- Bocchini, V. and Angeletti, P.U. (1969) Proc. Natl. Acad. Sci. U.S.A. 64, 787.
- McDonald, N.Q. et al. (1991) Nature 354, 411.
- Huang, E.J. and Reichardt, L.F. (2001) Annu. Rev. Neurosci. 24, 677.
- Freund, V. and Frossard, N. (1994) Prog. Brain Res. 146, 335.
- Raychaudhuri, S.P. and Raychaudhuri, S.K. (2004) Prog. Brain Res. 146, 433.
- Kawamoto, K. and Matsuda, H. (2004) Prog. Brain. Res. 146, 369.
- Teng, K.K. and Hempstead, B.L. (2004) Cell Mol. Life Sci. 61, 35.