|Reactivity||Human, Mouse, Rat|
|Calculated MW||27818 Da|
|Homology||Mouse, rat - 16/17 amino acid residues identical.|
|Other Names||Brain-derived neurotrophic factor, BDNF, Abrineurin, BDNF|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)DEDQKVRPNEENNKDAD, corresponding to amino acid residues 72-88 of human BDNF (precursor) (Accession P23560 ). Pro-domain of the BDNF protein.The antibody is specific for proBDNF, it does not crossreact with proNGF, proNT-3 or mature BDNF.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS) pH 7.4, 1% BSA, 0.025% NaN3.|
|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 water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of growth factors that includes nerve growth factor (NGF) neurotrophin-3 (NT-3) and neurotrophin-4/5 (NT-4/5). All neurotrophins are synthesized as preproneurotrophin precursors that are subsequently processed within the intracellular transport pathway to yield proneurotrophins that are further processed to generate the mature form. The mature form of BDNF is a non-covalent stable homodimer that can be secreted in both constitutive and regulated pathways. Until recently, the functional role of the neurotrophin prodomains were thought to include assistance in the correct folding of the mature protein and the sorting of the neurotrophins into the constitutive or regulated secretory pathway. However, a growing body of evidence suggests that the uncleaved proneurotrophin precursors can be secreted from cells and that they may mediate different biological functions. The functional importance of the prodomain of BDNF was recently demonstrated in a study showing that a polymorphism that replaces valine for methionine at position 66 of the pro domain, is associated with memory defects and abnormal hippocampal function in humans. Another recent study showed that the regulated extracellular cleavage of proBDNF to mature BDNF by plasmin is necessary for establishing late-phase long-term potentiation (L-LTP) a process that involves long-lasting changes in the structure and function of hippocampal synapses. Finally, proBDNF was shown to be decreased in the brains of patients suffering from Alzheimer’s disease. Mature BDNF binds to the specific tyrosine kinase receptor TrkB and to p75NTR, a member of the TNF receptor superfamily. ProBDNF can similarly bind both receptors although it appears to have a greater affinity for the p75NTR receptor. Abgent is pleased to offer a new antibody directed against a highly specific epitope located in the pro domain region of human BDNF. Anti-proBDNF (#AG1181) does not cross react with mature BDNF, pro and mature NGF or mature NT-3.
References 1. Lee R. et al. (2001) Science 294,1945. 2. Egan, M.F. et al. (2003) Cell 112, 257. 3. Pang, P.T. et al. (2004) Science 306, 487. 4. Michalski, B. et al. (2003) Mol. Brain Res. 111, 148.
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