Product Name: Amyloid Fibrils (OC)
Product Number: AB-NN194-1
| Size: | 25 µl | Price: | 89.00 | |
| $US |
Target Full Name: Alzheimer disease amyloid protein
Target Alias: OC; Fibrils; Amyloid Oligomer aß; A11; Amyloid beta A4 protein; ABPP; APPI; Cerebral vascular amyloid peptide; PreA4; Protease nexin-II; APP; A4; AD
Product Type Specific: Amyloid protein pan-specific antibody
Antibody Code: NN194-1
Antibody Target Type: Pan-specific
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Ig Isotype Clone: N/A
Antibody Immunogen Source: Fibrils prepared from human Aβ42 peptide
Production Method: Protein A purified
Target Alias: OC; Fibrils; Amyloid Oligomer aß; A11; Amyloid beta A4 protein; ABPP; APPI; Cerebral vascular amyloid peptide; PreA4; Protease nexin-II; APP; A4; AD
Product Type Specific: Amyloid protein pan-specific antibody
Antibody Code: NN194-1
Antibody Target Type: Pan-specific
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Ig Isotype Clone: N/A
Antibody Immunogen Source: Fibrils prepared from human Aβ42 peptide
Production Method: Protein A purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Storage Buffer: Phosphate buffered saline, 50% glycerol, 0.09% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | Immunohistochemistry | ICC/Immunofluorescence | Immunoprecipitation | ELISA | DB
Antibody Dilution Recommended: DB (1:1000); optimal dilutions for assays should be determined by the user.
Antibody Potency: Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrilllar oligomers or natively folded proteins.
Storage Buffer: Phosphate buffered saline, 50% glycerol, 0.09% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | Immunohistochemistry | ICC/Immunofluorescence | Immunoprecipitation | ELISA | DB
Antibody Dilution Recommended: DB (1:1000); optimal dilutions for assays should be determined by the user.
Antibody Potency: Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrilllar oligomers or natively folded proteins.
Antibody Species Reactivity: Human
Antibody Positive Control: A 1:1000 dilution of SPC-507 was sufficient for detection of amyloid fibrils on PVDF membranes using transferred fibrils by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.
Related Product 1: Amyloid Oligomers (A11) pan-specific antibody (Cat. No.: AB-NN198-1)
Antibody Positive Control: A 1:1000 dilution of SPC-507 was sufficient for detection of amyloid fibrils on PVDF membranes using transferred fibrils by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.
Related Product 1: Amyloid Oligomers (A11) pan-specific antibody (Cat. No.: AB-NN198-1)
Scientific Background: Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. Many degenerative diseases are known to be related to the accumulation of misfolded proteins as amyloid fibres (1, 2). These include the amyloid-β peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimer’s symptomology, the deposition of α-synuclein in the Lewy bodies of Parkinson’s disease, and accumulation of polyglutamine-containing aggregates in Huntington’s disease (2, 3).
References
[1] Glabe C.G. (2004) Trends Biochem Sci. 29(10): 542-547.
[2] Kayed R. et al. (2004) J Bio. Chem. 279: 46363-46366.
[3] Kayed R. et al. (2003) Science. 300(5618): 486-489.
[1] Glabe C.G. (2004) Trends Biochem Sci. 29(10): 542-547.
[2] Kayed R. et al. (2004) J Bio. Chem. 279: 46363-46366.
[3] Kayed R. et al. (2003) Science. 300(5618): 486-489.
© Kinexus Bioinformatics Corporation 2017