|Reactivity||Human, Mouse, Rat|
|Calculated MW||27077 Da|
|Other Names||Beta-nerve growth factor, Beta-NGF, Ngf, Ngfb|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Highly purified 2.5 S mouse NGF (Accession P01139).The antibody does not react with BDNF, NT-3, and NT-4/5.|
|Peptide Confirmation||Confirmed by SDS-PAGE and bioassay.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml of sterile deionized water, depending on the sample size. The antibody was aliquoted in sterile conditions.|
|Antibody Concentration After Reconstitution||0.3 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 5% sucrose (no preservative).|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl 5 mM acetic acid.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1-3 µg antigen per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
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 The biological effects of NGF are mediated by two receptors: TrkA, which is specific for NGF, and p75, which binds all the neurotrophins.12
References 1. Roux, P. et al. (2002) Prog. Neurobiol. 67, 203. 2. Levi-Montalcini, R. (1966) Harvey Lect. 60, 217. 3. Farinas, I. et al. (1998) Neuron 21, 325. 4. Levi-Montalcini, R.et al. (1996) Trends Neurosci. 19, 514. 5. Bradshaw, R.A. (1978) Ann. Rev. Biochem 47, 191. 6. Bocchini, V. and Angeletti, P.U. (1969) Proc. Natl. Acad. Sci. USA 64, 787. 7. McDonald, N.Q.et al. (1991) Nature 354, 411. 8. Huang, E.J. and Reichardt, L.F. (2001) Annu. Rev. Neurosci. 24, 677. 9. Freund V. and Frossard, N. (1994) Prog. Brain Res. 146, 335. 10. Raychaudhuri, S.P. and Raychaudhuri, S.K. (2004) Prog. Brain Res. 146, 433. 11. Kawamoto, K. and Matsuda, H. (2004) Prog. Brain. Res. 146, 369. 12. Teng, K.K. and Hempstead, B.L. (2004) Cell Mol. Life Sci. 61, 35.
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