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Proteins and peptidesAnti-Ly6g antibody [1A8] - mouse IgG2c (Chimeric)
Low endotoxin, Azide free.
Our first-to-market chimera with mouse IgG2c backbone, this functional antibody specifically depletes neutrophils in vivo for up to 72h.
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Rabbit Recombinant Monoclonal Amyloid-beta precursor protein antibody - conjugated to Alexa Fluor® 647. Suitable for IHC-Fr and reacts with Human samples. Cited in 1 publication.
IgG
Rabbit
Alexa Fluor® 647
Ex: 650nm, Em: 665nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Monoclonal
IHC-Fr | |
---|---|
Human | Tested |
Mouse | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info - | Notes - |
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 Cu(2+)-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 Cu(2+) 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 Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), 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).
Amyloid-beta precursor protein, APP, ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II, CVAP, PN-II, APP, A4, AD1
Rabbit Recombinant Monoclonal Amyloid-beta precursor protein antibody - conjugated to Alexa Fluor® 647. Suitable for IHC-Fr and reacts with Human samples. Cited in 1 publication.
Amyloid-beta precursor protein, APP, ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II, CVAP, PN-II, APP, A4, AD1
IgG
Rabbit
Alexa Fluor® 647
Ex: 650nm, Em: 665nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Monoclonal
mOC64
Affinity purification Protein A
This antibody reacts weakly with beta Amyloid 1-40.
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle, Store in the dark
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
Amyloid beta 1-42 plays a central role in synaptic activity and neuronal health. While not inherently pathogenic its tendency to aggregate forms oligomers and fibrils which become toxic to neurons. This peptide contributes to synaptic dysfunction and neuronal cell death and is a major component of extracellular amyloid plaques found in brain tissue. Within the cellular environment amyloid beta 1-42 can interact with receptors membrane lipids and intracellular signaling mechanisms thereby affecting neuronal cell function.
Beta Amyloid 1-42 often referred to as Abeta 42 or amyloid beta 1-42 is a peptide derived from the amyloid precursor protein (APP). This peptide consists of 42 amino acids and has a molecular weight of approximately 4.5 kDa. It is predominantly found in the brain especially within regions associated with memory and cognitive function. Beta amyloid 1-42 is a product of enzymatic cleavage by beta and gamma secretases from the larger APP molecule. Due to its aggregation-prone nature beta amyloid 1-42 is a focus in neuroscience research particularly concerning the formation of amyloid plaques.
Amyloid beta 1-42 is important in the amyloidogenic pathway which is one of the critical components in APP processing. The pathway includes proteolytic enzymes like beta secretase (BACE1) and gamma secretase where misregulation may lead to excessive production or deposition of amyloid beta peptides. Another related pathway is the tau protein phosphorylation pathway which indirectly interacts with amyloid beta 1-42 due to shared signaling intermediates impacting tau stabilization and microtubule assembly in neurons.
Amyloid beta 1-42 plays a pivotal role in Alzheimer's disease a prevalent neurodegenerative disorder. The excessive accumulation of beta amyloid in the form of plaques is a hallmark of the disease contributing to cognitive decline. Also it has links to cerebral amyloid angiopathy where it deposits in the walls of blood vessels of the central nervous system. Both conditions may involve interactions with tau protein another pathological feature of Alzheimer's disease which undergoes hyperphosphorylation leading to neurofibrillary tangles formation.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
IHC image of beta Amyloid 1-42 staining in a section of frozen human Alzheimer brain*.
The section was fixed using 10% formaldehyde in 1XPBS for 10 minutes. No antigen retrieval step was performed prior to staining. Non-specific protein-protein interactions were then blocked in TBS containing 0.025% (v/v) Triton X-100, 0.3M (w/v) glycine and 1% (w/v) BSA for 1h at room temperature. The section was then incubated overnight at +4°C in TBS containing 0.025% (v/v) Triton X-100 and 1% (w/v) BSA with ab224025 at 1/100 dilution (shown in red) and counterstained using ab195887, Mouse monoclonal to alpha Tubulin (Alexa Fluor® 488), at 1/250 dilution (shown in green). Nuclear DNA was labelled with DAPI (shown in blue). The section was then mounted using Fluoromount®.
Image was taken with a confocal microscope (Leica-Microsystems, TCS SP8).
For other IHC staining systems (automated and non-automated), customers should optimize variable parameters such as antigen retrieval conditions, antibody concentrations and incubation times.
*Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
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