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Amyloid beta Antibody / APP

SKU: orb2636345

Description

Proteolytic cleavage of the Amyloid protein precursor (APP) gives rise to the b-Amyloid and Amyloid A4 proteins, which are present in human platelets. Amyloid deposition is associated with type II diabetes, Down syndrome and a variety of neurological disorders, including Alzheimer s disease. The Amyloid precursor protein (APP) undergoes alternative splicing, resulting in several isoforms. Proteolytic cleavage of APP leads to the formation of the 4 kDa Amyloid b/A4 Amyloid protein. This protein is involved in the formation of neurofibrillary tangles and plaques that characterize the senile plaques of Alzheimer s patients. APLP1 (Amyloid precursor-like protein 1) and APLP2 are structurally similar to APP. Human APLP2 is a membrane-bound sperm protein that contains a region highly homologous to the transmembrane-cytoplasmic domains of APP found in brain plaques of Alzheimer s disease patients.

Images & Validation

Tested ApplicationsIHC-P
Dilution RangeImmunohistochemistry (FFPE): 1-2ug/ml
ReactivityHuman
Application Notes
Optimal dilution of the Beta Amyloid antibody should be determined by the researcher.

Key Properties

Antibody TypePrimary Antibody
HostMouse
ClonalityMonoclonal
IsotypeMouse IgG1, kappa
Clone No.APP/4469
ImmunogenAmino acids 1-17 of the amyloid beta protein was used as the immunogen for the Beta Amyloid antibody. This antibody recognizes an epitope in the region of amino acids 8-16 of the amyloid precursor protein.
ConjugationUnconjugated

Storage & Handling

StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
Expiration Date12 months from date of receipt.
Hazard InformationThis Beta Amyloid antibody is available for research use only.
DisclaimerFor research use only

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UniProt Details

No UniProt data available

Protocol Information

IHC-P
Immunohistochemistry Paraffin
View Protocol

Available Sizes

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20 μg
$ 410.00
Free Secondary Antibody (20 ul)0/0

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