| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB9710-SP | |||
| Carrier Free | FAB9710V-100UG | |||
| Carrier Free | FAB9710U-100UG | |||
| Carrier Free | FAB9710T-100UG | |||
| Carrier Free | FAB9710S-100UG | |||
| Carrier Free | FAB9710R-100UG | |||
| Carrier Free | FAB9710N-100UG | |||
| Carrier Free | FAB9710G-100UG | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-97930-0.025ml | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB96182-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB9618R-SP | |||
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Alexa Fluor 350 | FAB890U-100UG | |||
| Alexa Fluor 405 | FAB890V-100UG | |||
| Alexa Fluor 488 | FAB890G-100UG | |||
| Alexa Fluor 532 | FAB890X-100UG | |||
| Alexa Fluor 594 | FAB890T-100UG | |||
| Alexa Fluor 647 | FAB890R-100UG | |||
| Alexa Fluor 700 | FAB890N-100UG | |||
| Alexa Fluor 750 | FAB890S-100UG | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB890-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB96181-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB9618-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB96181R-SP | |||
![Western Blot: Amyloid Oligomers Antibody [NBP1-97930] - Western blot analysis of Human Abeta42 fibrils and prefibrillar oligomers showing detection of Amyloid Oligomers Oligomers (A11) protein using Rabbit Anti-Amyloid Oligomers Oligomers (A11) Polyclonal Antibody (NBP1-97930). Primary Antibody: Rabbit Anti-Amyloid Oligomers Oligomers (A11) Polyclonal Antibody (NBP1-97930) at 1:1000. Courtesy of: Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489. doi: 10.1126/science.1079469.](http://images.novusbio.com/fullsize/Amyloid-Oligomers-Antibody-Western-Blot-NBP1-97930-img0007.jpg "Western Blot: Amyloid Oligomers Antibody [NBP1-97930] - Western blot analysis of Human Abeta42 fibrils and prefibrillar oligomers showing detection of Amyloid Oligomers Oligomers (A11) protein using Rabbit Anti-Amyloid Oligomers Oligomers (A11) Polyclonal Antibody (NBP1-97930). Primary Antibody: Rabbit Anti-Amyloid Oligomers Oligomers (A11) Polyclonal Antibody (NBP1-97930) at 1:1000. Courtesy of: Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489. doi: 10.1126/science.1079469.")
![Western Blot: beta Amyloid 42 Peptide [NBP3-18318] - Western blot of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right) using anti-amyloid beta 6E10 antibody. Amyloid beta constructs at 160 pmol were run on 4-12% Bis-Tris SDS-PAGE, transferred to nitrocellulose in the presence of 0.02% v/v Tween-20, and blotted with 1:1000 mouse 6E10 primary antibody (Biolegend). Oligomers observed under TEM/AFM show distinct dimer/trimer bands as well as a signal from ~37-75 kDa (middle). Fibrils observed under TEM/AFM show a signal greater than 100 kDa and a distinct signal in the stacking gel (right).](http://images.novusbio.com/fullsize/beta-Amyloid-42-Peptide-Western-Blot-NBP3-18318-img0001.jpg "Western Blot: beta Amyloid 42 Peptide [NBP3-18318] - Western blot of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right) using anti-amyloid beta 6E10 antibody. Amyloid beta constructs at 160 pmol were run on 4-12% Bis-Tris SDS-PAGE, transferred to nitrocellulose in the presence of 0.02% v/v Tween-20, and blotted with 1:1000 mouse 6E10 primary antibody (Biolegend). Oligomers observed under TEM/AFM show distinct dimer/trimer bands as well as a signal from ~37-75 kDa (middle). Fibrils observed under TEM/AFM show a signal greater than 100 kDa and a distinct signal in the stacking gel (right).")
![In vitro assay: beta Amyloid 42 Peptide [NBP3-18318] - Amyloid beta 1-42 oligomers and fibrils show a dose-dependent toxicity to primary rat cortical neurons, but not monomers (NBP3-18318). Survival of rat primary cortical neurons 14 days after treatment with different concentrations of (A) monomers, (B) oligomers or (C) fibrils quantified by MAP2 positive neurons and expressed as a percentage of control. Fibrils and respective vehicle controls were initially sonicated in a Bioruptor. Test conditions were run in the same plate as untreated control and vehicle controls, which consisted of buffer without amyloid beta 1-42 protein. Data expressed as mean +/- s.e.m. (n=6). A global analysis of the data was performed using a one-way ANOVA followed by Dunnetts test; ** p<0.01 stats vs control; ## p<0.01, #### p<0.0001 stats vs vehicle control.](http://images.novusbio.com/fullsize/beta-Amyloid-42-Peptide-In-vitro-assay-NBP3-18318-img0002.jpg)
![Immunomicroscopy: beta Amyloid 42 Peptide [NBP3-18318] - AFM of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right). Atomic force microscopy analysis of 1.0 mg/mL samples diluted to 0.1 mg/mL in dH2O, mounted on freshly cleaved mica, washed, dried and analyzed with tapping mode. Representative images are 2.5 x 2.5 m x-y with a z-range of 10 nm.](http://images.novusbio.com/fullsize/beta Amyloid 42 Peptide-Immunomicroscopy-NBP3-18318-img0004.jpg)
![Electron Microscopy: beta Amyloid 42 Peptide [NBP3-18318] - TEM of amyloid beta 1-42 monomers (NBP3-18318, left), oligomers (middle) and fibrils (right). Negative stain transmission electron microscopy images acquired at 80 Kv on carbon coated 400 mesh copper grids using phosphotungstic acid and uranyl acetate stain. Scale bar = 100 nm.](http://images.novusbio.com/fullsize/beta-Amyloid-42-Peptide-Electron-Microscopy-NBP3-18318-img0003.jpg)
![Western Blot: APP Antibody [NB300-308]](http://images.novusbio.com/fullsize/APP-Antibody-Western-Blot-NB300-308-img0001.jpg "Western Blot: APP Antibody [NB300-308]")
![Immunocytochemistry/Immunofluorescence: APP Antibody [NB300-308] - Cell surface staining of VDR (green) on live neurons followed by fixation and immunofluorescence labeling of target protein (100x) APP. Overlay images indicate the possible co-localization of VDR/APP on the neuronal plasma membrane. Image collected and cropped by CiteAb from the following publication (//journals.plos.org/plosone/article?id=10.1371/journal.pone.0188605) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APP-Antibody-Immunocytochemistry-Immunofluorescence-NB300-308-img0002.jpg)
![Western Blot: APP Antibody [NB300-308] - Cell surface staining of VDR (green) on live neurons followed by fixation & immunofluorescence labeling of target proteins (100x): A) ADAM10; B) APP; C) BACE1; D) Nicastrin; E) Presenilin 1; F) Presenilin 2. Overlay images indicate the possible co-localization of VDR/ADAM10 (A) or VDR/APP (B) or VDR/Nicastrin (D) or limited co-localization of VDR/ Presenilin 1 (E) on the neuronal plasma membrane. Overlay images do not indicate co-localization for VDR/BACE1 (C) or VDR/Presenilin 2 (F) on the neuronal plasma membrane. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29176823), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-308_rabbit-polyclonal-app-antibody-31020241533495.jpg)
