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Storage instructions Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage buffer Preservative: 0.02% Sodium Azide
Constituents: 50% Glycerol, PBS (without Mg 2+ and Ca 2+), 150mM Sodium chloride, pH 7.4
Concentration information loading...
Purity Immunogen affinity purified
Purification notes ab65159 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/500 - 1/1000. Detects a band of approximately 65 kDa (predicted molecular weight: 65 kDa).
Function Inhibits fibrillization of beta amyloid peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin.
Tissue specificity Expressed predominantly in brain. Deposited preferentially in primitive or neuritic amyloid plaques which are typical of Alzheimer disease.
Sequence similarities Contains 7 collagen-like domains.
Post-translational modifications Undergoes proteolytic cleavage by furin protease to yield the soluble collagen-like Alzheimer amyloid plaque component. Glycosylated. Hydroxylated on 11% of proline residues and 49% of lysine residues.
Cellular localization Membrane. After proteolytic cleavage, CLAC is secreted.
Information by UniProt
Alzheimer disease amyloid associated protein antibody
Alzheimer disease amyloid-associated protein antibody
Anti-CLACP antibody images
Western blot - CLACP antibody (ab65159)
All lanes : Anti-CLACP antibody (ab65159) at 1/500 dilution Lane 1 : Jurkat cell extract Lane 2 : A549 cell extract Lane 3 : A549 cell extract with immunising peptide at 10 µg Lysates/proteins at 30 µg per lane. Predicted band size : 65 kDa Observed band size : 65 kDa Additional bands at : 23 kDa,34 kDa,45 kDa,50 kDa,90 kDa. We are unsure as to the identity of these extra bands.
References for Anti-CLACP antibody (ab65159)
has not yet been referenced specifically in any publications.
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