Skip to main content

Anti-Abeta-42 Antibody, oligomeric (VIA) (C15-1317-404)

Sigma-Aldrich

Catalog No.
C15-1317-404
Manufacturer No.
ABN1650
Manufacturer Name
Sigma-Aldrich
Quantity
100
Unit of Measure
UL
Price: $687.43
List Price: $763.81

Amyloid beta A4 protein (UniProt P05067 also known as ABPP, Alzheimer disease amyloid protein, Amyloid precursor protein, APP, APPI, Cerebral vascular amyloid peptide, CVAP, PN-II, PreA4, Protease nexin-II) is encoded by the APP (also known as A4,

Enjoy exclusive benefits including discounted pricing on orders by contacting our Sales Executives to open an account.

Adding to cart… The item has been added

General description

Amyloid beta A4 protein (UniProt P05067; also known as ABPP, Alzheimer disease amyloid protein, Amyloid precursor protein, APP, APPI, Cerebral vascular amyloid peptide, CVAP, PN-II, PreA4, Protease nexin-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID 351) in human. Amyloid precursor protein (APP) is initially produced with a signal peptide sequence (a.a. 1-17), the removal of which yields the mature protein with a large extracellular portion (a.a. 18-699), followed by a transmembrane segment (a.a. 700-723) and a cytoplasmic (a.a. 724-770) tail. APP can be further processed by the α-, β-, and γ-secretases in two alternative processing pathways. In the non-amyloidogenic pathway, APP is first cleaved by the plasma membrane-localized α-secretase to generate an N-terminal extracellular sAPPα fragment (a.a. 18-687) and a membrane-bound C-terminal fragment C83 (CTFα), which can be further cleaved by γ-secretase to produce a non-toxic small peptide p3 and a cytoplasmic APP intracellular domain (AICD). In the amyloidogenic pathway, APP undergoes β-cleavage in BACE-1 (β-site APP-cleaving enzyme)-enriched endosomes to generate an N-terminal extracellular sAPPβ fragment (a.a. 18-671) and a membrane-bound C-terminal fragment C99 (CTFβ). Subsequent cleavage of C99 by γ-secretase releases the amyloid β peptides, Aβ1-42 (672-713) & Aβ1-40 (672-711), and AICD. Aβ accumulation in the cortical and hippocampal regions of the brain is a major pathological feature of Alzheimer′s disease (AD). Growing evidences implicate soluble oligomers as the more toxic species and the extent of oligomer formation and assembly correlates better with disease progression and cognitive dysfunction. These Aβ oligomers are able to induce other aggregation-prone proteins, including α-synuclein (α-syn), prion protein (PrP), and TDP-43, to assume oligomeric conformations. These proteins can then seed tau aggregation, resulting in neurodegeneration.

Specificity

This polyclonal antiserum (VIA) recognizes a distinct epitope specific to Aβ-42 oligomers. VIA does not recognize classic amyloid plaques composed of fibrillar Aβ or Aβ-40 (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Immunogen

Aggregated synthetic hexapeptide VIAVIA composed of two copies of Aβ-42 C-terminal end 3-amino acid sequence (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Application

Anti-Aβ-42, oligomeric (VIA), Cat. No. ABN1650, is a highly specific rabbit polyclonal antibody that targets oligomeric amyloid beta 42 and has been tested in Dot Blot, Immunofluorescence, Immunohistochemistry, and Western Blotting.

Immunofluorescence Analysis: A 1:150 dilution from a representative lot detected oligomeric Aβ-42, but not oligomeric Tau or large amyloid plaques in Alzheimer′s diseased (AD) human brain cryosections (Courtesy of Riddhi U Bodani, Kayed lab, Univ of Texas Medical Branch, Galveston, U.S.A.).

Immunohistochemistry Analysis: A 1:150 dilution from a representative lot detected oligomeric Aβ-42 immunoreactivity in Alzheimer′s diseased (AD) human cortex cryosections (Courtesy of Riddhi U Bodani, Kayed lab, Univ of Texas Medical Branch, Galveston, U.S.A.).

Dot Blot Analysis: A representative lot detected recombinant Aβ-42, but not Aβ-40, oligomers (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Immunofluorescence Analysis: A representative lot immunostained both prefibrillar and fibrillar Aβ-42 oligomers in Alzheimer′s diseased (AD) human brain (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Immunofluorescence Analysis: A representative lot detected oligomeric Aβ-42, but not amyloid plaques in coronal sections of Tg2576AD mice harboring human Swedish mutation APP (APPK670/671L) transgene (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Immunohistochemistry Analysis: A representative lot immunostained intracellular perinuclear Aβ-42 aggregates, but not amyloid plaques in Alzheimer′s diseased (AD) human brain (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Immunohistochemistry Analysis: A representative lot detected oligomeric Aβ-42 immunoreactivity in the hippocampus CA1 region of Tg2576AD mice harboring human Swedish mutation APP (APPK670/671L) transgene (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Western Blotting Analysis: A representative lot detected oligomeric A -42, but not monomeric Aβ-42, monomeric or oligomeric Aβ-40 (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).

Note: Both purified antibody (Cat. No. ABN1665) and unpurified antiserum (Cat. No. ABN1650) are suitable for Dot blot, immunofluorescence, immunohistochemistry, and Western blotting applications. However, we recommend using only the purified antibody for neutralization studies.

Research Category
Neuroscience

Quality

Evaluated by Dot Bot analysis of Aβ proteins.

Dot Blot Analysis: A 1:150 dilution of this antiserum detected recombinant Aβ-42, but not Aβ-40, oligomer.

Target description

Variable depending on the sizes of the Aβ-42 oligmers.

Physical form

Rabbit polyclonal antibody serum with 0.05% sodium azide.

Unpurified.

Storage and Stability

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

biological source: rabbit. Quality Level: 100. antibody form: serum. antibody product type: primary antibodies. clone: polyclonal. species reactivity: human. technique(s): dot blot: suitable, immunofluorescence: suitable, immunohistochemistry: suitable, western blot: suitable. UniProt accession no.: P05067. shipped in: ambient. target post-translational modification: unmodified. Gene Information: human ... APP(351). Storage Class Code: 12 - Non Combustible Liquids. WGK: WGK 1. Flash Point(F): Not applicable. Flash Point(C): Not applicable.
UPC:
51202901
Condition:
New
Weight:
1.00 Ounces
HazmatClass:
No
WeightUOM:
LB
MPN:
ABN1650


Cenmed Satisfaction Guarantee

At Cenmed, your confidence and satisfaction are paramount. We guarantee the quality and reliability of our extensive range of clinical and laboratory supplies. If you're not completely satisfied with your purchase, we offer a straightforward return process and dedicated support to resolve your concerns promptly. Our commitment ensures that you can order with confidence, knowing that Cenmed is dedicated to superior service and customer satisfaction. Trust us to meet your needs with every order, backed by our promise of excellence. Learn more in Help & FAQs.


"Cenmed provides me access to the same products/services normally reserved for much larger labs than mine. I was presently surprised by their product offering."

LAB DIRECTOR


"We utilized Cenmed's capabilities for a variety of projects around the world. They are a valued partner and supplier."

PHARMACEUTICAL SUPPLY CHAIN LEADER


"The reps are very good at finding products for customers in this period of supply chain issues."

SCOTT BEHMAN


"Your customer service has been excellent and makes me excited about purchasing with Cenmed in the future!!"

PROCUREMENT + BILLING COORDINATOR AT PHARMA.