app

APP/Protease nexin-II Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 101 kDa and the accession number is P05067-8.

Beta-amyloid 38/Beta-APP38 Protein, Human, Recombinant (aa 672-709, His & GST) is expressed in E. coli expression system with His and GST tag. The predicted molecular weight is 32.1 kDa and the accession number is P05067-1.

Beta-amyloid 40/Beta-APP40 Protein, Human, Recombinant (His & GST) is expressed in E. coli expression system with His and GST tag. The predicted molecular weight is 31.8 kDa and the accession number is P05067-1.

Beta-amyloid 42/Beta-APP42 Protein, Human, Recombinant (His & GST) is expressed in E. coli expression system with His and GST tag. The predicted molecular weight is 32.4 kDa and the accession number is P05067-1.

Beta-amyloid 39/Beta-APP39 Protein, Human, Recombinant (aa 672-710, His & GST) is expressed in E. coli expression system with His and GST tag. The predicted molecular weight is 32.2 kDa and the accession number is P05067-1.

Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes.

BACE1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 49.8 kDa and the accession number is P56818.

BACE2, also known as beta secretase 2, belongs to the peptidase A1 family. It is a protease known to be an important enzyme involved in the cellular pathways. BACE2 has been shown to interact with GGA1 and GGA2. It is the major β-secretase in vivo. BACE2 is located on chromosome 21 and may play a role in alzheimer's disease pathogenesis in down syndrome(DS). Overexpression of BACE2 by lentivirus markedly reduced amyloid β protein production in primary neurons. Despite an extra copy of the BACE2 gene in DS and the increase of its transcription, BACE2 protein levels are unchanged.

BACE1 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 49 kDa and the accession number is A0A024R3D7.

BACE1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 49.9 kDa and the accession number is A0A024R3D7.

BACE1 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 75 kDa and the accession number is A0A024R3D7.

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis. Cathepsin B Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 54.6 kDa and the accession number is P07858.

Pappalysin-2/PAPP-A2 is the second member of the pappalysin family of metzincin superfamily, of which PAPP-A is the first member. There is no homology between the prepro-peptides of PAPP-A and PAPP-A2, but 46% of the residues of mature PAPP-A are also present in mature PAPP-A2. PAPP-A specifically cleaves insulin-like growth factor-binding protein(IGFBP)-4, one of six known modulators of IGF-I and –II, whereas PAPP-A2 specifically cleaved IGFBP-5 at one site, between Ser-143 and Lys-144. In contrast to the cleavage of IGFBP-4 by PAPP-A that strictly requires the presence of IGF, the cleavage of IGFBP-5 by PAPP-A2 was IGF-independent. Recent data firmly establish PAPP-A and IGFBP-4 as an important functional pair in several systems. Because of its close relationship with PAPP-A, both structurally and functionally, PAPP-A2 is a likely candidate for IGFBP-5 proteinase in many tissues and conditioned media where IGFBP-5 proteolysis has been reported.

Immunoglobulin Kappa is constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.

Kappa-Casein (CSN3) is a secreted protein that belongs to the Kappa-Casein family. CSN3 exists in heteromultimers that are composed of alpha-s 1casein and kappa casein linked by disulfide bonds. CSN3 is involved in a number of important physiological processes. In the gut, CSN3 protein is split into an insoluble peptide (para kappa-casein) and a soluble hydrophilic glycopeptide (caseinomacropeptide). Caseinomacropeptide is responsible for increased efficiency of digestion, prevention of neonate hypersensitivity to ingested proteins, and inhibition of gastric pathogens. Kappa-casein also stabilizes micelle formation, preventing casein precipitation in milk.

May play a role in the regulation of immune cell function. Cytokine that imparts cellular protection against viral infection in a species-specific manner. Activates the interferon-stimulated response element signaling pathway. It is able to directly modulate cytokine release from monocytes and dendritic cells. Binds heparin.

Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. IAPP Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 31.4 kDa and the accession number is P10997.

Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.

Mal d 1 Protein, Apple, Recombinant is expressed in P. pastoris yeast expression system. The predicted molecular weight is 18.4 kDa.

Tumor necrosis factor receptor superfamily member 21(DR6) is a single-pass type I membrane protein and contains 1 death domain and 4 TNFR-Cys repeats. The protein may activate NF-kappa-B and promote apoptosis and it may activate JNK and be involved in T-cell differentiation.It is required for both normal cell body death and axonal pruning. 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). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).

Probable Xaa-Pro Aminopeptidase 3 (XPNPEP3) is a member of the peptidase M24B family. XPNPEP3 has two isoforms and both are widely expressed. XPNPEP3 is localized in the Mitochondrion. XPNPEP3 catalyzes the release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Defects in XPNPEP3 are the cause of nephronophthisis-like nephropathy type 1 which is a disorder with features of nephronophthisis, a cystic kidney disease leading to end-stage renal failure.

Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration.

Aminopeptidase P (APP) is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. A membrane-bound and soluble form of this enzyme (XPNPEP2) have been identified as products of two separate genes. XPNPEP2, the X-linked gene that encodes membranous aminopeptidase P (APP), has been reported to associate with APP activity. The membrane aminopeptidase P (XPNPEP2) is largely limited in distribution to endothelia and brush border epithelia. APP and XPNPEP2 contain homologous blocks of sequence common to members of the pita bread-fold protein family, of which Escherichia coli methionine aminopeptidase is the prototype. The C-2399A variant in XPNPEP2 is associated with reduced APP activity and a higher incidence of AE-ACEi. XPNPEP2 mRNA was detected in fibroblasts that carry the translocation, suggesting that this gene at least partially escapes X inactivation. XPNPEP2 is a candidate gene for premature ovarian failure (POF).

Amyloid β A4 Precursor Protein-Binding Family A Member 3 (APBA3) is an adapter protein that belongs to the X11 family. APBA3 contains 2 PDZ (DHR) domains and 1 PID domain and interacts with the Alzheimer's disease amyloid precursor protein.. APBA3 is believed to be involved in signal transduction processes. Unlike X11-α and -β which are generally neuronal proteins, APBA3 is widely expressed in all tissues examined with lower levels in brain and testis. It binds to the cytoplasmic domain of amyloid protein (APP) in vivo and may modulate processing of the β-amyloid precursor protein (APP) and hence formation of β-APP.

Plays a role as a neuroprotective factor. Protects against neuronal cell death induced by multiple different familial Alzheimer disease genes and amyloid-beta proteins in Alzheimer disease. Mediates its neuroprotective effect by interacting with a receptor complex composed of IL6ST/GP130, IL27RA/WSX1 and CNTFR. Also acts as a ligand for G-protein coupled receptors FPR2/FPRL1 and FPR3/FPRL2. Inhibits amyloid-beta protein 40 fibril formation. Also inhibits amyloid-beta protein 42 fibril formation. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Also suppresses apoptosis by binding to BID and inhibiting the interaction of BID with BAX and BAK which prevents oligomerization of BAX and BAK and suppresses release of apoptogenic proteins from mitochondria. Forms fibers with BAX and also with BID, inducing BAX and BID conformational changes and sequestering them into the fibers which prevents their activation. Can also suppress apoptosis by interacting with BIM isoform BimEL, inhibiting BimEL-induced activation of BAX, blocking oligomerization of BAX and BAK, and preventing release of apoptogenic proteins from mitochondria. Plays a role in up-regulation of anti-apoptotic protein BIRC6/APOLLON, leading to inhibition of neuronal cell death. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death. Competes with importin KPNB1 for binding to IGFBP3 which is likely to block IGFBP3 nuclear import. Induces chemotaxis of mononuclear phagocytes via FPR2/FPRL1. Reduces aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPR2 to APP. Protects retinal pigment epithelium (RPE) cells against oxidative stress-induced and endoplasmic reticulum (ER) stress-induced apoptosis. Promotes mitochondrial biogenesis in RPE cells following oxidative stress and promotes STAT3 phosphorylation which leads to inhibition of CASP3 release. Also reduces CASP4 levels in RPE cells, suppresses ER stress-induced mitochondrial superoxide production and plays a role in up-regulation of mitochondrial glutathione. Reduces testicular hormone deprivation-induced apoptosis of germ cells at the nonandrogen-sensitive stages of the seminiferous epithelium cycle. Protects endothelial cells against free fatty acid-induced inflammation by suppressing oxidative stress, reducing expression of TXNIP and inhibiting activation of the NLRP3 inflammasome which inhibits expression of proinflammatory cytokines IL1B and IL18. Protects against high glucose-induced endothelial cell dysfunction by mediating activation of ERK5 which leads to increased expression of transcription factor KLF2 and prevents monocyte adhesion to endothelial cells. Inhibits the inflammatory response in astrocytes. Increases the expression of PPARGC1A/PGC1A in pancreatic beta cells which promotes mitochondrial biogenesis. Increases insulin sensitivity.

It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate. Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation. In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage.

NRBF2 (Nuclear Receptor Binding Factor 2) is a Protein Coding gene. The encoded protein may modulate transcriptional activation by target nuclear receptors. It is widely expressed in the appendix, placenta, and other tissues. NRBF2/Atg38 has been identified as the fifth subunit of the macroautophagy/autophagy class III phosphatidylinositol 3-kinase (PtdIns3K) complex, along with ATG14/Barkor, BECN1/Vps30, PIK3R4/p150/Vps15, and PIK3C3/Vps34. NRBF2 is a critical molecular switch of PtdIns3K and autophagy activation, and its on/off state is precisely controlled by MTORC1 through phosphorylation. NRBF2, a key component, and regulator of the PtdIns3K has been involved in APP-CTFs homeostasis in Alzheimer's disease (AD) cell models. NRBF2 plays an important role in regulating the degradation of APP-CTFs through modulating autophagy.

Insulin-Degrading Enzyme (IDE) is a secreted enzyme that belongs to the peptidase M16 family. IDE is a large zinc-binding protease and cleaves multiple short polypeptides that vary considerably in sequence. IDE plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling. IDE degrades amyloid formed by APP and IAPP. IDE may participate in the degradation and clearance of naturally secreted amyloid β-protein by neurons and microglia. IDE, which migrates at 110 kDa during gel electrophoresis under denaturing conditions, has since been shown to have additional substrates, including the signaling peptides glucagon, TGF α and β-endorphin.

Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. APBA2 Protein, Human, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 87.5 kDa and the accession number is Q99767.

RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs. Plays a role in the regulation of mRNA stability, alternative splicing and translation. Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA. Many of the target mRNAs are coding for RNA-binding proteins, transcription factors and proteins involved in RNA processing and/or neuronal development and function. By binding to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes to the stabilization of mRNA molecules and their protection from decay. Also binds to the polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing its affinity for mRNA binding. Mainly plays a role in neuron-specific RNA processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of other neuronal proteins, thereby contributing to the differentiation of neural progenitor cells, nervous system development, learning and memory mechanisms. Involved in the negative regulation of the proliferative activity of neuronal stem cells and in the positive regulation of neuronal differentiation of neural progenitor cells. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone of the hippocampus by binding to and stabilizing SATB1 mRNA. Binds and stabilizes MSI1 mRNA in neural stem cells. Exhibits increased binding to ACHE mRNA during neuronal differentiation, thereby stabilizing ACHE mRNA and enhancing its expression. Protects CDKN1A mRNA from decay by binding to its 3'-UTR. May bind to APP and BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization. Plays a role in neurite outgrowth and in the establishment and maturation of dendritic arbors, thereby contributing to neocortical and hippocampal circuitry function. Stabilizes GAP43 mRNA and protects it from decay during postembryonic development in the brain. By promoting the stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite outgrowth. Binds to BDNF long 3'UTR mRNA, thereby leading to its stabilization and increased dendritic translation after activation of PKC. By increasing translation of BDNF after nerve injury, may contribute to nerve regeneration. Acts as a stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby increasing its translation and enhancing its functional activity in neuron-specific splicing. Stimulates translation of mRNA in a poly(A)- and cap-dependent manner, possibly by associating with the EIF4F cap-binding complex. May also negatively regulate translation by binding to the 5'UTR of Ins2 mRNA, thereby repressing its translation. Upon glucose stimulation, Ins2 mRNA is released from ELAVL4 and translational inhibition is abolished. Also plays a role in the regulation of alternative splicing. May regulate alternative splicing of CALCA pre-mRNA into Calcitonin and Calcitonin gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR for binding to U-rich intronic sequences of CALCA pre-mRNA.

Plays a role as a neuroprotective factor. Protects against neuronal cell death induced by multiple different familial Alzheimer disease genes and amyloid-beta proteins in Alzheimer disease. Mediates its neuroprotective effect by interacting with a receptor complex composed of IL6ST/GP130, IL27RA/WSX1 and CNTFR. Also acts as a ligand for G-protein coupled receptors FPR2/FPRL1 and FPR3/FPRL2. Inhibits amyloid-beta protein 40 fibril formation. Also inhibits amyloid-beta protein 42 fibril formation. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Also suppresses apoptosis by binding to BID and inhibiting the interaction of BID with BAX and BAK which prevents oligomerization of BAX and BAK and suppresses release of apoptogenic proteins from mitochondria. Forms fibers with BAX and also with BID, inducing BAX and BID conformational changes and sequestering them into the fibers which prevents their activation. Can also suppress apoptosis by interacting with BIM isoform BimEL, inhibiting BimEL-induced activation of BAX, blocking oligomerization of BAX and BAK, and preventing release of apoptogenic proteins from mitochondria. Plays a role in up-regulation of anti-apoptotic protein BIRC6/APOLLON, leading to inhibition of neuronal cell death. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death. Competes with importin KPNB1 for binding to IGFBP3 which is likely to block IGFBP3 nuclear import. Induces chemotaxis of mononuclear phagocytes via FPR2/FPRL1. Reduces aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPR2 to APP. Protects retinal pigment epithelium (RPE) cells against oxidative stress-induced and endoplasmic reticulum (ER) stress-induced apoptosis. Promotes mitochondrial biogenesis in RPE cells following oxidative stress and promotes STAT3 phosphorylation which leads to inhibition of CASP3 release. Also reduces CASP4 levels in RPE cells, suppresses ER stress-induced mitochondrial superoxide production and plays a role in up-regulation of mitochondrial glutathione. Reduces testicular hormone deprivation-induced apoptosis of germ cells at the nonandrogen-sensitive stages of the seminiferous epithelium cycle. Protects endothelial cells against free fatty acid-induced inflammation by suppressing oxidative stress, reducing expression of TXNIP and inhibiting activation of the NLRP3 inflammasome which inhibits expression of proinflammatory cytokines IL1B and IL18. Protects against high glucose-induced endothelial cell dysfunction by mediating activation of ERK5 which leads to increased expression of transcription factor KLF2 and prevents monocyte adhesion to endothelial cells. Inhibits the inflammatory response in astrocytes. Increases the expression of PPARGC1A/PGC1A in pancreatic beta cells which promotes mitochondrial biogenesis. Increases insulin sensitivity.

Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration.

Mannose-binding Lectin (MBL) is an acute phase protein bearing to the family of collectins produced by the liver as a monomer that forms a triple helix. Once released in serum, it further polymerizes forming dimers to octamers. The degree of serum polymerization is critical for the biological activity of MBL. MBL has higher affinity to microbial polysaccharides or their glycoconjugates. MBL was shown earlier to bind cell surfaces of bacteria, fungi, protozoa and viruses and acts as an acute-phase plasma protein (APP) during infection and inflammation. MBL activates the lectin-complement pathway, promotes opsonophagocytosis and modulates inflammation.

Amyloid precursor protein (APP) is a type I membrane protein with several isoforms due to alternative splicing, performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Of the three major splice isoforms of APP (APP695, APP751, and APP770) APP695 is the predominant neuronal form from which Amyloid beta peptide and transcriptionally-active cleaved intracellular domain of APP (AICD) are preferentially generated by selective processing through the amyloidogenic pathway. Human APP695 consists of a 17 amino acid (aa) signal sequence, a 607 aa extracellular domain (ECD), a 24 aa transmembrane domain, and a 47 aa cytoplasmic domain. Within the ECD, human APP695 shares 97% aa sequence identity with mouse and rat APP695. Amyloid beta is a major molecule implicated in pathogenesis of Alzheimer's disease (AD) and related dementias. AICD regulates expression by direct promoter binding of multiple genes, including APP itself, the beta-secretase, BACE-1 and the Amyloid beta-degrading enzyme, Neprilysin. As such, APP695 plays an important role in brain development, learning and memory, synaptic plasticity, and neurodegeneration including AD.

Integral Membrane Protein 2B (ITM2B) is expressed in the Golgi and on the cell surface. ITM2B forms homodimer through disulfide-linked interaction with SPPL2A, SPPL2B and APP. ITM2B is expressed in brain and the other tissues. Defects in ITM2B cause cerebral amyloid angiopathy ITM2B-related type 1(CAA-ITM2B1) and amyloid angiopathy ITM2B-related type 2(CAA-ITM2B2). CAA-ITM2B1 is characterized by amyloid deposition in the walls of cerebral blood vessels and neurodegeneration in the central nervous system. CAA-ITM2B2 characterized by amyloid deposition in the walls of the blood vessels of the cerebrum, choroid plexus, cerebellum, spinal cord and retina.

TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. Mature human TREM-2  consists of a 156 amino acid (aa) extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. TREM-2 forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding (PubMed:10799849). Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia.

Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. Cathepsin D Protein, Rat, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 45.2 kDa and the accession number is P24268.

Gastrokine 1 (GKN1) belongs to the BRICHOS domain family and plays a major role in maintaining gastric mucosa integrity. GKN1 is highly expressed in gastric tissue and is secreted into the stomach but is not expressed in gastric cancer. GKN1-mediated inhibition of APP processing might represent a new approach for the prevention and therapy of Alzheimer's disease (AD). In the presence of GKN2, GKN1 loses its ability to decrease cell proliferation, induce apoptosis, and inhibit epigenetic alterations in gastric cancer cells, that GKN2 may contribute to the homeostasis of gastric epithelial cells by inhibiting GKN1 activity. The loss of GKN1 function contributes to malignant transformation and proliferation of gastric epithelial cells in gastric carcinogenesis.