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APLP1 encodes a member of the highly conserved amyloid precursor protein gene family. Additionally we are shipping APLP1 Antibodies (47) and APLP1 Proteins (6) and many more products for this protein.
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These data reveal a conserved mechanism for the binding of APP (show APP ELISA Kits)-family proteins to HS and imply a specific regulatory role of HS modifications in the biology of APP (show APP ELISA Kits) and APP-like (show APP ELISA Kits) proteins.
APLP1 and APLP2 (show APLP2 ELISA Kits), behave similarly to APP (show APP ELISA Kits) in that they both associate with assembled NMDA receptors in the endoplasmic reticulum
CSF (show CSF2 ELISA Kits) levels of 3 endogenous peptides derived from APLP1 (APL1beta25, APL1beta27 and APL1beta28) were decreased in Down syndrome.
APLP1 has a regulatory role in the nuclear translocation of APP (show APP ELISA Kits) family intracellular domains due to the sequestration of Fe65 (show APBB1 ELISA Kits).
[review] APP (show APP ELISA Kits) and its mammalian homologs, amyloid precursor-like proteins APLP1 and APLP2 (show APLP2 ELISA Kits), participate under physiological conditions via trans-cellular dimerization in synaptogenesis.
APLP1 binds the II-III loop of the Ca(v)2.3 calcium channel and that this binding promotes internalization of the channel.
Both APLP1 and APLP2 (show APLP2 ELISA Kits), form transcriptionally active triple protein complexes with Mint3 (show APBA3 ELISA Kits) and transcriptional co-activators Taz (show TAZ ELISA Kits) andYap.
Human cerebrospinal fluid contains three APLP1-derived Abeta (show APP ELISA Kits)-like peptides that are generated by beta- and gamma-cleavages at a concentration of approximately 4.5 nM.
APLP1 and APLP2 (show APLP2 ELISA Kits) are processed by the gamma-secretase in a Presenilin 1 (show PSEN1 ELISA Kits)-dependent manner and the extreme carboxyl-terminal fragments produced by this processing (APP-like (show APP ELISA Kits) Intracellular Domain) are able to enhance Fe65 (show APBB1 ELISA Kits)-dependent gene activation
APLP1 does not undergo the same type of regulated processing as APP (show APP ELISA Kits) and APLP2 (show APLP2 ELISA Kits).
Results suggest that APLP1 deficiency on its own does not lead to defects in synaptic plasticity, but affects synaptic transmission and network inhibition in the dentate gyrus
[review] A role of APP (show APP ELISA Kits) and its two closely related homologues APLP1 and APLP2 (show APLP2 ELISA Kits) has been determined in various aspects of nervous system development and function, in particular, for synapse formation and function.
findings demonstrated that NB-2 (show CNTN5 ELISA Kits) interacts with APLP and that both NB-2 (show CNTN5 ELISA Kits) and APLP1 are localized at presynaptic sites, suggesting that NB-2 (show CNTN5 ELISA Kits) associates with APLP1 in a cis (show CISH ELISA Kits) manner on the presynaptic membrane
Crystal structure of the E2 domain of amyloid precursor protein-like (show APP ELISA Kits) protein 1 in complex with sucrose octasulfate.
The 5' UTR (show UTS2R ELISA Kits) of the Aplp1 gene lacks any type of CAGA (show S100A8 ELISA Kits) box. This may explain its inability to form amyloid plaques.
Cytoplasmic polyadenylation element (CPE (show CPE ELISA Kits)) binding factor binds the small intracellular domain (ICD) of APLP1.
The results demonstrated that cell viability and neurite outgrowth of N2a cells undergoing knockdown of Aplp1 were significantly reduced, compared with N2a cells undergoing knockdown of either App (show APP ELISA Kits) or Aplp2 (show APLP2 ELISA Kits).
This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described.
amyloid-like protein 1
, amyloid beta (A4) precursor-like protein 1
, amyloid-like protein 1-like
, amyloid precursor-like protein 1