Technical Data
A2275-86Q
APP, Phosphorylated (Thr668) (Amyloid beta A4 Protein, ABPP, APPI, Alzheimer Disease Amyloid Protein, Cerebral Vascular Amyloid Peptide, CVAP, PreA4, Protease Nexin-II, PN-II, A4, AD1)
Description:
Amyloid beta (A4) Precursor Protein (APP) is a ubiquitously expressed transmembrane protein that is sequentially cleaved by beta-secretase and gamma-secretase to release extracellular peptides such as the b-amyloid peptides, which are deposited in the brain in Alzheimer's disease. APP exists in several isoforms ranging from 100-140kD, and is phosphorylated on various residues within the extracellular and cytoplasmic domains, effecting the proteolytic processing and secretion of the protein. Threonine 668 can be phosphorylated by cyclin-dependent kinase 5 (cdk5), GSK-3b and JNK, and may play an important role in neurite outgrowth of differentiating neurons.

Applications:
Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 0.1-1ug/ml
Optimal dilutions to be determined by the researcher.

Positive Control:
CAD cells transfected with wild type vs. T668A mutant APP

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
25ug-20CBlue IceHumanRabbit
Concentration:
As reported
Immunogen:
Synthetic phosphopeptide corresponding to the region of human APP that contains threonine 668 (corresponding to the APP695 isoform).
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in PBS, 0.02% sodium azide.
Specificity:
Recognizes human APP when phosphorylated at Thr668. Species Crossreactivity: mouse, rat, and frog.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Selkoe, DJ. et al. Trends Cell. Biol. 8(11), 447 (1998). 2.Tarr, PE. et al. J. Biol. Chem. 277(19), 16798 (2002).