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- 2025年08月05日
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- 文献和实验
- 技术资料
- 抗体名：
Purified (azide-free) anti-APP C-Terminal Fragment
- 抗体英文名：
Purified (azide-free) anti-APP C-Terminal Fragment
- 规格：
200ul
Purified anti-APP C-Terminal Fragment Antibody (Previously Covance catalog#
SIG-39152)
C1/6.1
Catalog# / Size 802801 / 200 µL
Clone
Regulatory Status RUO
Other Names AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2, Amyloid beta A4 protein, preA4,
protease nexin-II, peptidase nexin-II, beta-amyloid peptide, alzheimer disease amyloid protein,
cerebral vascular amyloid peptide, APP, Amyloid Precursor Protein
Previously Covance Catalog# SIG-39152
Isotype Mouse IgG1
Description APP functions as a cell surface receptor and performs physiological functions on the surface
of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. It is involved in
cell mobility and transcription regulation through protein-protein interactions and cleaved either
by alpha-secretase, beta-secretase or theta-secretase, leading to generation and extracellular
release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of
corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent
processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major
secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated
gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 and
amyloid-beta 42, major components of amyloid plaques, and the cytotoxic C-terminal
fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor betaamyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including
the beta-amyloid X-15 peptides, produced from the cleavage by alpha-secretase and all
terminating at Gln-686.
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文献和实验Measuring APP Carboxy-Terminal Fragments
cleaving enzyme (BACE1) near the C-terminus results in the formation of the APP C-terminal fragment (CTF) C99, a substrate for subsequent cleavage by γ-secretase to generate Aβ. Alternatively, APP cleavage by α-secretase to generate the APP CTF C83 occurs
The N-terminal and C-terminal portions of the heavy chain fragment C from botulinum neurotoxin serotype C [rBoNT(HC )] were expressed in Pichia pastoris and purified by ion-exchange chromotography (IEC). The N-terminal fragment, rBoNTC(Hc )-N
C-Terminal Sequence Analysis of 2DE-Separated Proteins
of proteins separated by two-dimensional polyacrylamide gel electrophoresis (2DE). For each purified protein, a peptide mixture is generated by cleavage of the protein with cyanogen bromide. During incubation with carboxypeptidases only the original C-terminal
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