Human Anti-Aβ Recombinant Antibody (clone 1E8-4b) (CAT#: VS-0423-CJ2)

• Host Species
• Human

• Type
• Mouse IgG

• Specificity
• Human Aβ

• Species Reactivity
• Human

• Clone
• 1E8-4b

• Conjugate
• Unconjugated

• Related Disease
• Alzheimer's disease (AD)

• Purity
• >95% as determined by SDS-PAGE

• Buffer
• PBS

• Storage
• Store at 4°C for short term. Aliquot and store at -20°C for long term. Avoid repeated freeze/thaw cycles.

• Application Notes
• ELISA: 0.1 μg/mL-10 μg/mL
  Immunohistochemistry: 10 μg/mL-20 μg/mL
  Western blot: 5 μg/mL

• Alternative Names
• Abeta; Amyloid beta

• Gene ID
• 351

• UniProt ID
• P05067

• Sequence Similarities
• Belongs to the APP family.

• Cellular Localization
• Amyloid, Cell membrane, Cell projection, Coated pit, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus, Secreted

• Post Translation Modifications
• Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF50, gamma-CTF57 and gamma-CTF59. PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro) (PubMed:30630874).
  Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE (PubMed:11604391, PubMed:16154999).
  Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686.
  Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either CASP6, CASP8 or CASP9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides.

• Protein Refseq
• NP_000475.1; NP_001129488.1; NP_001129601.1; NP_001129602.1; NP_001129603.1

• Function
• Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912).
  Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity).
  Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity).
  By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (PubMed:17062754, PubMed:23011729).
  Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu2+-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu2+ ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.
  Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu2+ and Fe3+ to Cu+ and Fe2+, respectively. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts.
  Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.
  The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
  N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).

Isotype Control

• MRO-A1591-YJ
• Mouse IgG Isotype control, Polyclonal

Secondary Antibody

• 2ND-040CQ
• Goat Anti-Mouse IgG (H&L) Antibody

• 2ND-042CQ
• Rabbit Anti-Mouse IgG (H&L) Antibody

Recommended Dilution Buffer

• MRO-0253YJ
• Reconstitution Buffer PBS