Anti-Drebrin (mAb)

  • Applications
    • ICC
    • IHC
    • IP
    • WB
  • Target Drebrin
  • Host Species Mouse
  • Species Reactivities Bovine, Cat, Chicken, Human, Mouse, Rat
  • Code # D029-3
  • Size 100 μg
  • Price
    $306.33
Specifications

Alternative Names

DBN1 drebrin 1, D0S117E drebrindrebrin E drebrin-1 drebrin E2 developmentally-regulated brain protein

Background

In developing neuronal tissue, various functional molecules appear timingly and influence the processes of cell differentiation, migration, neurite outgrowth, and synaptic formation. Drebrins (developmentally regulated brain proteins) are candidates of such functional molecules, because they were expressed peculiarly in the course of development of neuronal tissues. Drebrin proteins are classified into an embryonic form (E) and an adult form (A) in mammals. The embryonic form is further classified into E1 and E2 in the chicken.
  • Antibody Type:
    Monoclonal
  • Application:
    ICC, IHC, IP, WB
  • Clone Number:
    M2F6
  • Conjugate:
    Unlabeled
  • Description:
    Monoclonal antibody of 100 μg targeting Drebrin for ICC, IHC, IPP, WB.
  • Formulation:
    100 µg IgG in 100 µl volume of PBS containing 50% glycerol, pH 7.2. No preservative is contained.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Gene ID (Rat):
  • Host Species:
    Mouse
  • Immunogen:
    Purified chicken drebrin E
  • Isotype:
    IgG
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts with DrebrinE andDrebrin Aon Western blotting, Immunoprecipitation,Immunohistochemistry and Immunocytochemistry.
  • Research Area:
    Neuroscience
  • Short Description:
    Drebrin Monoclonal Antibody.
  • Size:
    100 μg
  • Species Reactivity:
    Bovine, Cat, Chicken, Human, Mouse, Rat
  • Storage Temperature:
    -20°C
  • Target:
    Drebrin
Citations
  1. Allison DW, et al., Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: maintenance of core components independent of actin filaments and microtubules. J Neurosci. 20, 4545-4554 (2000),
  2. Chew CS, et al., Drebrin E2 is differentially expressed and phosphorylated in parietal cells in the gastric mucosa. Am J Physiol Gastrointest Liver Physiol. 289, G320-31 (2005),
  3. Chew CS, et al., IQGAPs are differentially expressed and regulated in polarized gastric epithelial cells. Am. J. Physiol. Gastrointest Liver Physiol. 288, G376-G387 (2005),
  4. Counts SE, et al., Hippocampal drebrin loss in mild cognitive impairment. Neurodegener Dis.10, 216-219 (2012),
  5. Fucini RV, et al., Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1. Mol Biol Cell. 13, 621-631 (2002),
  6. Hayashi K and Shirao T. Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. J. Neurosci. 19, 3918-3925 (1999),
  7. Hayashi K, et al., Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex. J Neurosci. 16, 7161-7170 (1996),
  8. Keon BH, et al., Isoform specific expression of the neuronal F-actin binding protein, drebrin, in specialized cells of stomach and kidney epithelia. J Cell Sci. 113, 325-336 (2000),
  9. Kramer ML and Schulz-Schaeffer WJ. Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J Neurosci. 27, 1405-1410. (2007),
  10. Lacor PN, et al., Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci. 27, 796-807 (2007),
  11. Luna EJ, et al., Actin-binding membrane proteins identified by F-actin blot overlays. Soc Gen Physiol Ser. 52, 3-18 (1997),
  12. Peitsch WK, et al., Cell biological and biochemical characterization of drebrin complexes in mesangial cells and podocytes of renal glomeruli. J Am Soc Nephrol. 14, 1452-1463 (2003),
  13. Shapiro LA and Whitaker-Azmitia PM. Expression levels of cytoskeletal proteins indicate pathological aging of S100B transgenic mice: an immunohistochemical study of MAP-2, drebrin and GAP-43. Brain Res. 1019, 39-46 (2004),
  14. Shim KS and Lubec G. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci Lett. 324, 209-212 (2002),
  15. Shiraishi-Yamaguchi Y, et al., Interaction of Cupidin/Homer2 with two actin cytoskeletal regulators, Cdc42 small GTPase and Drebrin, in dendritic spines. BMC Neurosci. 10, 25 (2009),
  16. Shirao T and Obata K, Immunochemical homology of 3 developmentally regulated brain proteins and their developmental change in neuronal distribution. Brain Res. 394, 233-244 (1986),
  17. Takahashi H, et al., Activity of the AMPA receptor regulates drebrin stabilization in dendritic spine morphogenesis. J Cell Sci. 122, 1211-1219 (2009),
  18. Takahashi H, et al., Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis. J. Neurosci. 23, 6586-6595 (2003),
  19. Xu W and Stamnes M. The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin. J Biol Chem. 281, 11826-11833 (2006),
  20. Zhao L, et al., Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease. Nat Neurosci. 9, 234-242 (2006)
References
  1. Pérez-Martínez, M., et al., J. Cell. Sci. 123, 1160-1170 (2010) [WB]
  2. Takahashi, H., et al., J. Cell. Sci. 122, 1211-1219 (2009) [WB, IC]
  3. Kramer, M. L. and Schulz-Schaeffer W. J. J. Neurosci. 27, 1405-1410 (2007) [WB]
  4. Chew, C. S., et al., Am. J. Physiol. Gastrointest Liver Physiol. 289, G320-G331 (2005) [WB, IP, IC]
  5. Chew, C. S., et al., Am. J. Physiol. Gastrointest Liver Physiol. 288, G376-G387 (2005) [WB]
  6. Peitsch, W. K., et al., J. Am. Soc. Nephrol. 14, 1452-1463 (2003) [WB, IF, EM]
  7. Takahashi, H., et al., J. Neurosci. 23, 6586-6595 (2003) [WB]
  8. Allison, D. W., et al., J. Neurosci. 20, 4545-4554 (2000) [IC]
  9. Hayashi, K., and Shirao,T., J. Neurosci. 19, 3918-3925 (1999)[IC]
  10. Hayashi, K., et al., J. Neurosci. 16, 7161-7170 (1996) [WB, IP, IHC,EM]
  11. Shirao, T., et al., J. Biochem. 117, 231-236 (1995)
  12. Asada, H., et al., J. Neurosci. Res. 38, 149-159 (1994)
  13. Imamura, K., et al., Neurosci. Res. 13, 33-41 (1992) [WB, IHC]
  14. Shirao, T., et al., Dev. Brain Res. 29, 233-244 (1986) [WB, IHC]