Human Brain Extract: sc-364375

Human brain extract is a complex biological substance derived from the human brain tissue, encompassing a myriad of proteins, lipids, and other molecular constituents intrinsic to one of the most complex organs in the body. This extract is meticulously prepared by homogenizing brain tissue, followed by processes that might include filtration and centrifugation to isolate specific biochemical components. In research contexts, human brain extract has been instrumental in neurobiological studies, providing a rich source of native brain chemicals and pathways for examination. Researchers utilize this extract to delve into the fundamental aspects of brain function, such as neurotransmission, neural plasticity, and the biochemical underpinnings of memory and cognition. Additionally, it serves as a crucial tool in the study of neurodegenerative conditions, not for direct applications, but to understand the biochemical environment of diseased versus healthy neural tissues. The extract's use in proteomics and genomics provides insights into the expression patterns and interactions of brain-specific proteins, aiding in the mapping of complex neural networks. By offering a direct snapshot of the biochemical milieu of the brain, human brain extract facilitates a deeper understanding of its functional dynamics, aiding scientific exploration aimed at deciphering the vast complexities of the human brain.

Human Brain Extract References:

1. Human brain lectin: a soluble lectin that binds actin.  |  Joubert, R., et al. 1992. J Neurochem. 58: 200-3. PMID: 1309234
2. alpha B-crystallin is present in reactive glia in Creutzfeldt-Jakob disease.  |  Renkawek, K., et al. 1992. Acta Neuropathol. 83: 324-7. PMID: 1373027
3. Immunocytochemical detection of the growth-associated protein B-50 by newly characterized monoclonal antibodies in human brain and muscle.  |  Mercken, M., et al. 1992. J Neurobiol. 23: 309-21. PMID: 1385623
4. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation.  |  Liu, F., et al. 2005. Eur J Neurosci. 22: 1942-50. PMID: 16262633
5. A novel monoclonal antibody DC63 reveals that inhibitor 1 of protein phosphatase 2A is preferentially nuclearly localised in human brain.  |  Kovacech, B., et al. 2007. FEBS Lett. 581: 617-22. PMID: 17266954
6. SYNCRIP, a component of dendritically localized mRNPs, binds to the translation regulator BC200 RNA.  |  Duning, K., et al. 2008. J Neurochem. 105: 351-9. PMID: 18045242
7. A novel brain-specific 25 kDa protein (p25) is phosphorylated by a Ser/Thr-Pro kinase (TPK II) from tau protein kinase fractions.  |  Takahashi, M., et al. 1991. FEBS Lett. 289: 37-43. PMID: 1909972
8. Effects of the blocking agents bovine serum albumin and Tween 20 in different buffers on immunoblotting of brain proteins and marker proteins.  |  Wedege, E. and Svenneby, G. 1986. J Immunol Methods. 88: 233-7. PMID: 3514766
9. Identification of several forms of the glial fibrillary acidic protein, or alpha-albumin, by a specific monoclonal antibody.  |  Gheuens, J., et al. 1984. J Neurochem. 43: 964-70. PMID: 6206204
10. Mouse monoclonal antibodies reacting with human brain glial fibrillary acidic protein.  |  Albrechtsen, M., et al. 1984. J Neurochem. 42: 86-93. PMID: 6689701
11. The demonstration of new human brain-specific proteins by high-resolution two-dimensional polyacrylamide gel electrophoresis.  |  Jackson, P. and Thompson, RJ. 1981. J Neurol Sci. 49: 429-38. PMID: 7217993
12. Purification and characterization of a novel metalloprotease from human brain with the ability to cleave substrates derived from the N-terminus of beta-amyloid protein.  |  Schönlein, C., et al. 1994. Biochem Biophys Res Commun. 201: 45-53. PMID: 8198608
13. cDNA cloning of human N-Oct3, a nervous-system specific POU domain transcription factor binding to the octamer DNA motif.  |  Schreiber, E., et al. 1993. Nucleic Acids Res. 21: 253-8. PMID: 8441633