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Amyloid-beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Amyloid-beta precursor protein) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Gamma-CTF(50)); C31]

 A4_MACFA                Reviewed;         770 AA.
P53601; Q60HH7; Q95KN7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-FEB-2003, sequence version 3.
13-FEB-2019, entry version 147.
RecName: Full=Amyloid-beta A4 protein;
AltName: Full=ABPP;
Short=APP;
AltName: Full=Alzheimer disease amyloid A4 protein homolog;
AltName: Full=Amyloid precursor protein {ECO:0000305};
AltName: Full=Amyloid-beta precursor protein {ECO:0000305};
Contains:
RecName: Full=N-APP;
Contains:
RecName: Full=Soluble APP-alpha;
Short=S-APP-alpha;
Contains:
RecName: Full=Soluble APP-beta;
Short=S-APP-beta;
Contains:
RecName: Full=C99;
AltName: Full=Beta-secretase C-terminal fragment;
Short=Beta-CTF;
Contains:
RecName: Full=Amyloid-beta protein 42;
Short=Abeta42;
AltName: Full=Beta-APP42;
Contains:
RecName: Full=Amyloid-beta protein 40;
Short=Abeta40;
AltName: Full=Beta-APP40;
Contains:
RecName: Full=C83;
AltName: Full=Alpha-secretase C-terminal fragment;
Short=Alpha-CTF;
Contains:
RecName: Full=P3(42);
Contains:
RecName: Full=P3(40);
Contains:
RecName: Full=C80;
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 59;
AltName: Full=Gamma-CTF(59);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 57;
AltName: Full=Gamma-CTF(57);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 50;
AltName: Full=Gamma-CTF(50);
Contains:
RecName: Full=C31;
Flags: Precursor;
Name=APP; ORFNames=QccE-15949;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS APP695 AND APP770).
TISSUE=Cerebellum;
PubMed=1905108;
Podlisny M.B., Tolan D.R., Selkoe D.J.;
"Homology of the amyloid beta protein precursor in monkey and human
supports a primate model for beta amyloidosis in Alzheimer's
disease.";
Am. J. Pathol. 138:1423-1435(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain cortex;
Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
"Isolation and characterization of cDNA for macaque neurological
disease genes.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Functions as a cell surface receptor and performs
physiological functions on the surface of neurons relevant to
neurite growth, neuronal adhesion and axonogenesis. Interaction
between APP molecules on neighboring cells promotes
synaptogenesis. Involved in cell mobility and transcription
regulation through protein-protein interactions (By similarity).
Can promote transcription activation through binding to APBB1-KAT5
and inhibit Notch signaling through interaction with Numb (By
similarity). Couples to apoptosis-inducing pathways such as those
mediated by G(O) and JIP (By similarity). Inhibits G(o) alpha
ATPase activity (By similarity). Acts as a kinesin I membrane
receptor, mediating the axonal transport of beta-secretase and
presenilin 1 (By similarity). May be involved in copper
homeostasis/oxidative stress through copper ion reduction (By
similarity). In vitro, copper-metallated APP induces neuronal
death directly or is potentiated through Cu(2+)-mediated low-
density lipoprotein oxidation (By similarity). Can regulate
neurite outgrowth through binding to components of the
extracellular matrix such as heparin and collagen I and IV.
Induces a AGER-dependent pathway that involves activation of p38
MAPK, resulting in internalization of amyloid-beta peptide and
mitochondrial dysfunction in cultured cortical neurons. Provides
Cu(2+) ions for GPC1 which are required for release of nitric
oxide (NO) and subsequent degradation of the heparan sulfate
chains on GPC1 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P05067}.
-!- FUNCTION: Amyloid-beta peptides are lipophilic metal chelators
with metal-reducing activity. Binds transient metals such as
copper, zinc and iron (By similarity). {ECO:0000250}.
-!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved
peptides, including C31, are potent enhancers of neuronal
apoptosis. {ECO:0000250}.
-!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and
degeneration of both neuronal cell bodies (via caspase-3) and
axons (via caspase-6). {ECO:0000250}.
-!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several
cytoplasmic proteins, including APBB family members, the APBA
family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding
to DAB1 inhibits its serine phosphorylation (By similarity).
Interacts (via NPXY motif) with DAB2 (via PID domain); the
interaction is impaired by tyrosine phosphorylation of the NPXY
motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1,
KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro,
it binds MAPT via the MT-binding domains (By similarity).
Associates with microtubules in the presence of ATP and in a
kinesin-dependent manner (By similarity). Interacts, through a C-
terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7
in hippocampal neurons (By similarity). Amyloid-beta associates
with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21
and AGER (By similarity). Interacts with ITM2B. Interacts with
ITM2C. Interacts with IDE. Can form homodimers; dimerization is
enhanced in the presence of Cu(2+) ions. Can form homodimers; this
is promoted by heparin binding (By similarity). Amyloid-beta
protein 40 interacts with S100A9 (By similarity). CTF-alpha
product of APP interacts with GSAP (By similarity). Interacts with
SORL1 (By similarity). Interacts with PLD3 (By similarity).
Interacts with VDAC1 (By similarity). Interacts with NSG1; could
regulate APP processing (By similarity). Amyloid-beta protein 42
interacts with FPR2 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P05067, ECO:0000250|UniProtKB:P12023}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P05067}. Membrane
{ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P05067}. Perikaryon
{ECO:0000250|UniProtKB:P05067}. Cell projection, growth cone
{ECO:0000250|UniProtKB:P05067}. Membrane, clathrin-coated pit
{ECO:0000250|UniProtKB:P05067}. Early endosome
{ECO:0000250|UniProtKB:P05067}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:P05067}. Note=Cell surface protein that
rapidly becomes internalized via clathrin-coated pits. Only a
minor proportion is present at the cell membrane; most of the
protein is present in intracellular vesicles. During maturation,
the immature APP (N-glycosylated in the endoplasmic reticulum)
moves to the Golgi complex where complete maturation occurs (O-
glycosylated and sulfated). After alpha-secretase cleavage,
soluble APP is released into the extracellular space and the C-
terminal is internalized to endosomes and APP sorts to the
basolateral surface in epithelial cells. During neuronal
differentiation, the Thr-743 phosphorylated form is located mainly
in growth cones, moderately in neurites and sparingly in the cell
body. Casein kinase phosphorylation can occur either at the cell
surface or within a post-Golgi compartment. Associates with GPC1
in perinuclear compartments. Colocalizes with SORL1 in a vesicular
pattern in cytoplasm and perinuclear regions.
{ECO:0000250|UniProtKB:P05067}.
-!- SUBCELLULAR LOCATION: Soluble APP-beta: Secreted
{ECO:0000250|UniProtKB:P05067}.
-!- SUBCELLULAR LOCATION: Amyloid-beta protein 42: Cell surface
{ECO:0000250|UniProtKB:P05067}. Note=Associates with FPR2 at the
cell surface and the complex is then rapidly internalized.
{ECO:0000250|UniProtKB:P05067}.
-!- SUBCELLULAR LOCATION: Gamma-secretase C-terminal fragment 59:
Nucleus {ECO:0000250|UniProtKB:P05067}. Cytoplasm
{ECO:0000250|UniProtKB:P05067}. Note=located to both the cytoplasm
and nuclei of neurons. It can be translocated to the nucleus
through association with APBB1 (Fe65).
{ECO:0000250|UniProtKB:P05067}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=APP770;
IsoId=P53601-1; Sequence=Displayed;
Name=APP695;
IsoId=P53601-2; Sequence=VSP_000010, VSP_000011;
Name=3;
IsoId=P53601-3; Sequence=VSP_013360, VSP_013361;
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for
sorting of membrane proteins to the basolateral surface of
epithelial cells. {ECO:0000250|UniProtKB:P05067}.
-!- DOMAIN: The GFLD subdomain binds Cu(2+) ions; this promotes
homodimerization. {ECO:0000250|UniProtKB:P05067}.
-!- DOMAIN: The NPXY sequence motif found in many tyrosine-
phosphorylated proteins is required for the specific binding of
the PID domain. However, additional amino acids either N- or C-
terminal to the NPXY motif are often required for complete
interaction. The PID domain-containing proteins which bind APP
require the YENPTY motif for full interaction. These interactions
are independent of phosphorylation on the terminal tyrosine
residue. The YENPXY site is also involved in clathrin-mediated
endocytosis. {ECO:0000250|UniProtKB:P05067}.
-!- DOMAIN: The C-terminal region can bind zinc ions; this favors
dimerization and formation of higher oligomers.
{ECO:0000250|UniProtKB:P05067}.
-!- PTM: Proteolytically processed under normal cellular conditions.
Cleavage either by alpha-secretase, beta-secretase or theta-
secretase leads 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 protein 40 and amyloid-beta protein 42,
major components of amyloid plaques, and the cytotoxic C-terminal
fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59) (By
similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved by caspases during neuronal
apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9
results in the production of the neurotoxic C31 peptide and the
increased production of amyloid-beta peptides. {ECO:0000250}.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
serine residues is neuron-specific. Phosphorylation can affect APP
processing, neuronal differentiation and interaction with other
proteins (By similarity). {ECO:0000250}.
-!- PTM: Trophic-factor deprivation triggers the cleavage of surface
APP by beta-secretase to release sAPP-beta which is further
cleaved to release an N-terminal fragment of APP (N-APP).
{ECO:0000250}.
-!- PTM: Amyloid-beta peptides are degraded by IDE. {ECO:0000250}.
-!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and
zinc, can induce histidine-bridging between amyloid-beta molecules
resulting in amyloid-beta-metal aggregates. Extracellular zinc-
binding increases binding of heparin to APP and inhibits collagen-
binding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
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EMBL; M58726; AAA36828.1; -; mRNA.
EMBL; M58727; AAA36829.1; -; mRNA.
EMBL; AB125150; BAD51938.1; -; mRNA.
PIR; A49795; A49795.
RefSeq; XP_005548940.1; XM_005548883.2. [P53601-1]
RefSeq; XP_005548942.1; XM_005548885.2. [P53601-3]
RefSeq; XP_005548944.1; XM_005548887.2.
UniGene; Mfa.1063; -.
ProteinModelPortal; P53601; -.
SMR; P53601; -.
MEROPS; I02.015; -.
PRIDE; P53601; -.
Ensembl; ENSMFAT00000026579; ENSMFAP00000007885; ENSMFAG00000002479. [P53601-1]
Ensembl; ENSMFAT00000026583; ENSMFAP00000007889; ENSMFAG00000002479. [P53601-3]
GeneID; 101926433; -.
KEGG; mcf:101926433; -.
CTD; 351; -.
GeneTree; ENSGT00530000063252; -.
HOVERGEN; HBG000051; -.
KO; K04520; -.
OrthoDB; 953529at2759; -.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0051233; C:spindle midzone; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0030546; F:receptor activator activity; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
GO; GO:0002265; P:astrocyte activation involved in immune response; IEA:Ensembl.
GO; GO:0008088; P:axo-dendritic transport; ISS:UniProtKB.
GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0050890; P:cognition; ISS:UniProtKB.
GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB.
GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0007617; P:mating behavior; ISS:UniProtKB.
GO; GO:0014005; P:microglia development; IEA:Ensembl.
GO; GO:0090647; P:modulation of age-related behavioral decline; IEA:Ensembl.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:1905908; P:positive regulation of amyloid fibril formation; IEA:Ensembl.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
GO; GO:0061890; P:positive regulation of astrocyte activation; IEA:Ensembl.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IEA:Ensembl.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:1903980; P:positive regulation of microglial cell activation; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IEA:Ensembl.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IEA:Ensembl.
GO; GO:0032640; P:tumor necrosis factor production; IEA:Ensembl.
GO; GO:0008542; P:visual learning; ISS:UniProtKB.
CDD; cd00109; KU; 1.
Gene3D; 1.20.120.770; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
Gene3D; 4.10.230.10; -; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR036669; Amyloid_Cu-bd_sf.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
InterPro; IPR037071; Amyloid_glyco_Abeta_sf.
InterPro; IPR011178; Amyloid_glyco_Cu-bd.
InterPro; IPR024329; Amyloid_glyco_E2_domain.
InterPro; IPR008154; Amyloid_glyco_extra.
InterPro; IPR019744; Amyloid_glyco_extracell_CS.
InterPro; IPR015849; Amyloid_glyco_heparin-bd.
InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR036176; E2_sf.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103; PTHR23103; 1.
PANTHER; PTHR23103:SF7; PTHR23103:SF7; 1.
Pfam; PF10515; APP_amyloid; 1.
Pfam; PF12924; APP_Cu_bd; 1.
Pfam; PF12925; APP_E2; 1.
Pfam; PF02177; APP_N; 1.
Pfam; PF03494; Beta-APP; 1.
Pfam; PF00014; Kunitz_BPTI; 1.
PRINTS; PR00203; AMYLOIDA4.
PRINTS; PR00759; BASICPTASE.
PRINTS; PR00204; BETAAMYLOID.
SMART; SM00006; A4_EXTRA; 1.
SMART; SM00131; KU; 1.
SUPFAM; SSF109843; SSF109843; 1.
SUPFAM; SSF56491; SSF56491; 1.
SUPFAM; SSF57362; SSF57362; 1.
SUPFAM; SSF89811; SSF89811; 1.
PROSITE; PS00319; APP_CUBD; 1.
PROSITE; PS51869; APP_E1; 1.
PROSITE; PS51870; APP_E2; 1.
PROSITE; PS00320; APP_INTRA; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
2: Evidence at transcript level;
Alternative splicing; Amyloid; Apoptosis; Cell adhesion;
Cell membrane; Cell projection; Coated pit; Copper; Cytoplasm;
Cytoplasmic vesicle; Disulfide bond; Endocytosis; Endosome;
Glycoprotein; Heparin-binding; Iron; Isopeptide bond; Membrane;
Metal-binding; Notch signaling pathway; Nucleus; Phosphoprotein;
Protease inhibitor; Proteoglycan; Secreted; Serine protease inhibitor;
Signal; Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
SIGNAL 1 17 {ECO:0000250|UniProtKB:P05067}.
CHAIN 18 770 Amyloid-beta A4 protein.
/FTId=PRO_0000000101.
CHAIN 18 687 Soluble APP-alpha. {ECO:0000255}.
/FTId=PRO_0000000102.
CHAIN 18 671 Soluble APP-beta. {ECO:0000255}.
/FTId=PRO_0000000103.
CHAIN 18 286 N-APP. {ECO:0000250}.
/FTId=PRO_0000381967.
CHAIN 672 770 C99. {ECO:0000255}.
/FTId=PRO_0000000104.
CHAIN 672 713 Amyloid-beta protein 42. {ECO:0000255}.
/FTId=PRO_0000000105.
CHAIN 672 711 Amyloid-beta protein 40. {ECO:0000255}.
/FTId=PRO_0000000106.
CHAIN 688 770 C83. {ECO:0000255}.
/FTId=PRO_0000000107.
PEPTIDE 688 713 P3(42). {ECO:0000255}.
/FTId=PRO_0000000108.
PEPTIDE 688 711 P3(40). {ECO:0000255}.
/FTId=PRO_0000000109.
CHAIN 691 770 C80.
/FTId=PRO_0000384575.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
{ECO:0000255}.
/FTId=PRO_0000000110.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
{ECO:0000255}.
/FTId=PRO_0000000111.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
{ECO:0000255}.
/FTId=PRO_0000000112.
CHAIN 740 770 C31. {ECO:0000255}.
/FTId=PRO_0000000113.
TOPO_DOM 18 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 723 Helical. {ECO:0000255}.
TOPO_DOM 724 770 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 189 E1. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
DOMAIN 291 341 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DOMAIN 374 565 E2. {ECO:0000255|PROSITE-
ProRule:PRU01218}.
REGION 28 123 GFLD subdomain. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
REGION 96 110 Heparin-binding. {ECO:0000250}.
REGION 131 189 CuBD subdomain. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
REGION 181 188 Zinc-binding. {ECO:0000250}.
REGION 391 423 Heparin-binding. {ECO:0000250}.
REGION 491 522 Heparin-binding. {ECO:0000250}.
REGION 523 540 Collagen-binding. {ECO:0000250}.
REGION 732 751 Interaction with G(o)-alpha.
{ECO:0000250}.
MOTIF 724 734 Basolateral sorting signal.
{ECO:0000250}.
MOTIF 757 762 YENPXY motif; contains endocytosis
signal. {ECO:0000250|UniProtKB:P05067}.
COMPBIAS 230 260 Asp/Glu-rich (acidic).
COMPBIAS 274 280 Poly-Thr.
METAL 147 147 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
METAL 151 151 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
METAL 168 168 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
METAL 677 677 Copper or zinc 2.
{ECO:0000250|UniProtKB:P05067}.
METAL 681 681 Copper or zinc 2.
{ECO:0000250|UniProtKB:P05067}.
METAL 684 684 Copper or zinc 2.
{ECO:0000250|UniProtKB:P05067}.
METAL 685 685 Copper or zinc 2.
{ECO:0000250|UniProtKB:P05067}.
SITE 170 170 Required for Cu(2+) reduction.
{ECO:0000255|PROSITE-ProRule:PRU01217}.
SITE 301 302 Reactive bond. {ECO:0000250}.
SITE 671 672 Cleavage; by beta-secretase.
{ECO:0000250}.
SITE 672 673 Cleavage; by caspase-6. {ECO:0000250}.
SITE 687 688 Cleavage; by alpha-secretase.
{ECO:0000250|UniProtKB:P08592}.
SITE 690 691 Cleavage; by theta-secretase.
{ECO:0000250|UniProtKB:P08592}.
SITE 704 704 Implicated in free radical propagation.
{ECO:0000250}.
SITE 711 712 Cleavage; by gamma-secretase; site 1.
{ECO:0000250|UniProtKB:P08592}.
SITE 713 714 Cleavage; by gamma-secretase; site 2.
{ECO:0000250}.
SITE 720 721 Cleavage; by gamma-secretase; site 3.
{ECO:0000250}.
SITE 739 740 Cleavage; by caspase-3, caspase-6,
caspase-8 or caspase-9. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 206 206 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 497 497 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 729 729 Phosphothreonine.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 730 730 Phosphoserine; by APP-kinase I.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 757 757 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:P12023}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 38 62 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 73 117 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 98 105 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 133 187 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 144 174 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 158 186 {ECO:0000255|PROSITE-ProRule:PRU01217}.
DISULFID 291 341 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 300 324 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 316 337 {ECO:0000255|PROSITE-ProRule:PRU00031}.
CROSSLNK 763 763 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08592}.
VAR_SEQ 289 289 E -> V (in isoform APP695).
{ECO:0000303|PubMed:1905108}.
/FTId=VSP_000010.
VAR_SEQ 290 345 Missing (in isoform APP695).
{ECO:0000303|PubMed:1905108}.
/FTId=VSP_000011.
VAR_SEQ 345 345 M -> I (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_013360.
VAR_SEQ 346 364 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_013361.
CONFLICT 464 464 M -> T (in Ref. 2; BAD51938).
{ECO:0000305}.
SEQUENCE 770 AA; 87072 MW; 55712A39152690F6 CRC64;
MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK
TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG
EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE
EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC
RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQSLR KTTREPLTRD
PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA
KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL
QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER
MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET
KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN
IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN


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