Biosensis MOAB-2
Dear Doctor       Amyloid Beta 1-42 peptide

We would like to welcome you to our special September edition of Biosensis e-antibody solutions and introduce our new monoclonal to beta amyloid; MOAB-2: a new highly specific amyloid beta (Aβ) monoclonal antibody designed to facilitate and enhance research into Aβ neurotoxicity and its association with the neuropathology of Alzheimer's disease. (Image: Amyloid Beta 1-42 peptide http://randombio.com/alz.html).

 

The neurotoxicity of intraneuronal Aβ accumulation is an issue of considerable controversy today. Even the existence of Aβ intraneuronal deposits has recently been challenged by scientists, because of the lack of highly specific antibodies to Aβ which provide the clarity and staining definition that is sorely needed - until now. 

   

Biosensis is pleased to offer the monoclonal MOAB-2 (M-1586-100); A new pan-specific, high-titer antibody to Aβ residues 1-4 provides unparalleled staining clarity, stronger reactivity and greater sensitivity than any other Aβ monoclonal previously available for research. Click here to read more!

MOAB-2: Unprecedented features, unparalleled staining & clarity!
Western-blot analysis 1 Western-blot analysis 2
(Image: MOAB-2 does not detect APP in cell culture media, lysates and cortical brain extracts from 5xFAD mice. (A) Western-blot analysis of 5 μg or 15 μg cell lysates from HEK-APPSwe/BACE1 cells, probed with antibodies against C-terminus of APP (CT1565), N-terminus of APP (2211), Aβ (6E10, MOAB-2) or β-Actin (loading control). Notice all the other clones detect APP or APP-CTFs, but that MOAB-2 does not. (B) Western analysis of 25 μg total protein from detergent-extracted 5xFAD mouse cortex probed with 6E10 or MOAB-2 and β-Actin for loading control, demonstrating that MOAB-2 does not detect APP forms, unlike 6E10).

MOAB-2 does not cross react with APP or APP C-terminal fragments   

Unlike other monoclonals such as 6E10 and 4G8, MOAB-2 does not cross react with APP or APP C-terminal fragments, which allows isolation and localization of Aß protein from APP.

 

MOAB-2 preferentially detects pathogenic Aβ42 over Aβ40   

In dot blots, MOAB-2 recognizes all forms (unaggregated, oligometric, and fibrillar) of Aβ 42 protein and the unaggregated form of AB40. MOAB-2 is selective for the more neurotoxic Aβ42 compared to Aβ40. In titration tests, MOAB-2 demonstrated a 25 fold greater sensitivity of detection for the U-, O- and F-Aβ42 forms than for Aβ40, demonstrating it is a superb reagent for focusing in on the localization and function of Aβ42.

  

MOAB-2 is a superb immunohistochemical reagent for the localizing Aβ protein in vivo

Coronal sections  

Youmans et al. Molecular Neurodegeneration 2012, 7:8

(Image: Coronal sections of the frontal cortex from 1 and 3 month old 5xFAD mice immunostained with 6E10 and MOAB-2 and visualized via DAB staining. Notice how 6E10 is strongly immunoreactive across the field of the cortex, and at higher magnification shows that the cytoplasm is evenly stained with an immunonegative nuclei (A) indicating the detection of both APP and Aβ. In contrast, (B), MOAB-2 staining of sister sections is substantially less than for 6E10 and the intraneuronal staining is punctate. These results are consistent with MOAB-2 recognizing only Aβ and not APP. MOAB-2 reacts in IHC, IH(P) & IF, in all fixations from fresh frozen to archival paraffin embedded tissues.  

 

MOAB-2:Discover intraneuronal Aβ like never before possible, true clarity of staining  

  MOAB-2 Image 3 MOAB-2 Image 1 MOAB-2 Image 2                

(Image: MOAB-2 staining of senile plaque in human Alzheimer's diseased hippocampus formalin fixed paraffin embedded tissues with heat-induced antigen retrieval. Note the depth of clarity and lack of neuronal involvement).

  

MOAB-2 discriminates between APP and true intraneuronal Aβ in all its forms!

MOAB-2 detection    

(Image: MOAB-2 detection of intraneuronal Aβ and extracellular plaques in 5xFAD mouse brain tissues. Immunofluorescent detection of Aβ with MOAB-2 in the subiculum of (A) 1, 2 and 4 month old 5xFAD mice. Aβ accumulates extracellularly as the disease progresses making MOAB-2 the ideal reagent for studying both intraneuronal Aβ at early stages and extracellular Aβ at late stages seamlessly).

Biosensis is pleased to bring this new and exciting reagent to the market and we encourage all that have an interest in beta-amyloid or its pathology to try it.              

 When you want the best reagents, trust Biosensis 

 

The staff at Biosensis have many years of combined experience in manufacturing and working with antibodies and has published over 340 peer reviewed research publications in the field of neuroscience. We guarantee to provide you with the antibody information you need to get your research published.
BioSpeak

Each month, our Biospeak  e-bulletins highlight recent progress in important research areas such as:
  1. Avoiding manuscript rejection
  2. LRRK
  3. Insulin-like growth receptors
  4. Semaphorins
  5. Trk receptors
  6. Amyotrophic Lateral Sclerosis
  7. Motor Neuron Disease
  8. Neurotrophins
Quick Links

Apoptosis

Autophagy

Closing Headline
Web site guarantee logoShould your manuscript ever be rejected by ANY journal because of insufficient information about a Biosensis antibody, we will gladly refund TWICE the purchase price of that antibody!

By researchers for researchers!

If you have a query on any of our products, please contact us at biospeak@biosensis.com.
 
Sincerely,
Biosensis

Contact Information
Email: tina@avibiomail.com
Phone: + 61-43-166-5519
Web:
www.biosensis.com