943 Results for: "AbFrontier"

Supplier: AbFrontier

Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).

Supplier: AbFrontier

Dual specificity phosphatase 13(Also known as BEDP; MDSP; TMDP; SKRP4; DUSP13A; DUSP13B) is an enzyme that in humans is encoded by the DUSP13 gene.[1]
Members of the protein tyrosine phosphatase superfamily cooperate with protein kinases to regulate cell proliferation and differentiation. This superfamily is separated into two families based on the substrate that is dephosphorylated. One family, the dual specificity phosphatases (DSPs) acts on both phosphotyrosine and phosphoserine/threonine residues. This gene encodes different but related DSP proteins through the use of non-overlapping open reading frames, alternate splicing, and presumed different transcription promoters. Expression of the distinct proteins from this gene has been found to be tissue specific and the proteins may be involved in postnatal development of specific tissues. A protein encoded by the upstream ORF was found in skeletal muscle, whereas the encoded protein from the downstream ORF was found only in testis. In mouse, a similar pattern of expression was found. Multiple alternatively spliced transcript variants were described, but the full-length sequence of only some were determined.[1]

Supplier: AbFrontier

Anti-PTPRM Mouse Monoclonal Antibody [clone: T5-AF1A8]

Supplier: AbFrontier

Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Supplier: AbFrontier

The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 – 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1).

Supplier: AbFrontier

Glyceraldehyde-3-phosphate dehydrogenase(GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer of identical 37-kDa subunits. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, this ubiquitously expressed enzyme also displays other activities unrelated to its glycolytic function. GAPDH is reported to be involved in the processes of DNA replication, DNA repair, nuclear RNA export, membrane fusion and microtubule bundling. Other studies also provide evidence of GAPDH playing an essential part of the program of gene expression observed in apoptosis and as part of the cellular phenotype of age-related neurodegenerative diseases. On recent study, GAPDH has identified of the most oxidant sensitive cell proteins.

Supplier: AbFrontier

Anti-Peroxiredoxin 5 Rabbit Polyclonal Antibody

Supplier: AbFrontier

The Smad family of proteins are functioning in the transmission of extracellular signals in the TGF-β signaling pathway. Binding of a TGF-β superfamily ligands to extracellular receptors triggers phosphorylation of Smad2 at a Serine-Serine-Methionine-Serine (SSMS) motif at its C-terminus. Phosphorylated Smad2 is then able to form a complex with Smad4. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression.
In mammals, eight Smad proteins have been identified to date. The Smad family of proteins can be divided into three functional groups: the receptor-activated Smads (R-Smads), common mediator Smads (Co-Smads), and the inhibitory Smads (I-Smads). The R-Smads are directly phosphorylated by the activated type I receptors on their C-terminal Ser-Ser-X-Ser (SSXS) motif and include Smad1, Smad2, Smad3, Smad5, and Smad8. Smad2 and Smad3 are phosphorylated in response to TGF-β and activin, whereas Smad1, Smad5, and Smad8 are phosphorylated in response to BMP (Bone Morphogenetic Protein). This C-terminal phosphorylation allows R-Smad binding to Co-Smad, Smad4, and translocation to the nucleus where they regulate TGF-β target genes. Smad6 and Smad7 belong to the I-Smad which bind to the type I receptor or Smad4 and block their interaction with R-Smads.

Supplier: AbFrontier

Selenoprotein-P(SelP) is the major selenoprotein in human blood plasma and a transport protein which is carrying selenium to various extrahepatic tissues. Though its expression is detected in most tissues, highest amounts are produced by the liver, which secretes highly glycosylated SelP into plasma. Purification of human SelP yields two distinct isoforms with 61 and 55 kDa, differing in selenium content. SelP also has been shown to chelate heavy metals such as cadmium and mercury, and there are several evidences about its serum antioxidant capacity and protection against oxidative stress. Selenium deficiency predispose to several pathological condition such as cancer, coronary heart disease and liver necrosis although the biological function of SelP in various pathologic conditions has not been established.

Supplier: AbFrontier

Cyclin D3, ~34kDa, is a member of cyclin D family that promotes cell cycle progression to the DNA systhesis (S) phase. Cyclins complexed with cyclin-dependent kinases(CDKs) mediate phosphorylation of other proteins relevant to cell proliferation. D-type cyclins and their complexing CDKs phosphorylate the retinoblastoma gene product with influences transcription of growth-controlling genes. Cyclin D3 regulates cell proliferation during hematopoiesis, carcinogenesis, and may have function in the terminally differentiated cells. In recent studies, there is reports that cyclin D3 involves in multiple myeloma and malignant precursor T cells.

Supplier: AbFrontier

Ubiquitin carboxy-terminal h d l L1 hydrolase (UCHL1) is a deubiqutinating enzyme. Ubiquitin UCHL1, also known as PGP9.5, is a protein of 223 amino acids and one of the most abundant proteins in the brain (1-2% of the total soluble protein). Although it was originally characterized as a deubiquitinating enzyme recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. A large amount of mono-Ub is tightly associated with UCHL1, inhibiting the degradation of mono-Ub in the brain. The precise regulation of UCHL1 is essential for neurons to survive and to maintain their proper function. UCHL1 is involved in the pathogenesis of Parkinson's disease (PD) and Alzheimer's disease (AD). Down-regulation and extensive oxidative modification of UCHL1 have been observed in the brains of AD patients as well as PD patients. A post-translational modification of UCHL1 that controls the function of UCHL1 is mono-ubiquitination. It occurs reversibly to a lysine residue near the active site of UCHL1.

Supplier: AbFrontier

NF-κB (Nuclear Factor kappa B) is a nuclear transcription factor found in all cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, ultraviolet irradiation, and bacterial or viral antigens. NF-κB plays a key role in regulating the immune response to infection. Consistent with this role, incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection and improper immune development. There are five members in the NF-κB family: NF-κB1, NF-κB2, RelA (also named p65), RelB, and c-Rel.
The most common form of NF-κB is the p50/RelA heterodimer, although other forms of NF-κB dimers, such as p50/p50, p52/p52, p52/RelA, p50/c-Rel, c-Rel/c-Rel, p52/RelB, and p50/RelB, have also been identified in some types of cells.
The primary role of NF-κB is to maintain normal cellular functions that range from cell-to-cell communication to cell motility, cell cycle progression, and cell lineage development. The activity of NF-κB is tightly regulated by interaction with inhibitory IκB proteins.

Supplier: AbFrontier

Protein Phosphatase 2A (PP2A) is one of the major Ser/Thr phosphatases implicated in the regulation of many cellular processes including regulation of different signal transduction pathways, cell cycle progression, DNA replication, gene transcription and protein translation. The core structure comprises a 36 kDa catalytic subunit (PP2AC) and a 65 kDa regulatory subunit (PR65 or A subunit). Each PP2A subunit has at least two isoforms and the catalytic subunit, present in the α and β isoforms, share 97% homology. The differential association of all these subunits gives rise to an extensive subset of oligomeric holoenzymes. It is widely thought that PP2A exercises regulatory flexibility and differential substrate specificity through the specific association of the core dimer (PP2AD) with one of the three regulatory B subunits. Moreover, PP2A interacts with a still growing number of cellular and viral proteins and is regulated by posttranslational modifications.

Supplier: AbFrontier

Enolase (2-phosphogly-cerate hydrolyase or phosphopyruvate hydrates) is a glycolytic enzyme that catalyzes the dehydration and conversion of 2-phosphoglycerate to phosphoenolpyruvate. It comprises three distinct subunits, α, β and γ. The γγ and αγ dimeric forms of enolase, referred to as neuron-specific enolase(NSE), are localized mainly in neurons and neuroectodermal tissue. NSE has a high stability in biological fluids and can easily diffuse to the extracellular medium and cerebrospinal fluid(CSF) when neuronal membranes are injured. NSE is used clinically as a sensitive and useful marker of neuronal damage in several neurological disorders including stroke, hypoxic brain damage, status epilepticus, Creutzfeldt-Jakob disease, and herpetic encephalitis.

Supplier: AbFrontier

NCK1 is one of the adaptor proteins which mediate specific protein-protein interactions in signaling processes. Adaptor proteins usually contain several domains like SH2 (Src homology 2) and SH3 which allow specific interactions with other specific proteins.
NCK1 and NCK2 showing high sequence identity (68%) have three SH3 domains and a C-terminal SH2 domain. Both of them bind receptor tyrosine kinases such as PDGFR and other tyrosine phosphorylated
proteins via their SH2 domains. Various molecules which interact with SH domains of Nck and regulate signaling process of actin cytoskeleton reorganization have been identified. Ncks are thought to have important functions in the development of mesodermal structures during embryogenesis, linked to a role in cell movement and cytoskeletal reorganization.
Nck also have a function in modulating mRNA translation at the level of initiation by interacting eukayotic initiation factor 2 (eIF2). Under the stressed conditions, protein synthesis is reduced by inhibiting the activity of eIF2 through the phosphorylation, transiently inhibiting recycling of eIF2
into its active form.

Supplier: AbFrontier

Peptidoglycan recognition proteins (PGRPs) are pattern recognition molecules that recognize bacteria and their unique cell wall component, peptidoglycan (PGN).
Mammals have four PGRPs, designated in humans PGRP-S(24kDa), PGRP-L(60~65kDa), PGRP-Iα(38kDa), and PGRP-Iβ(44kDa). Human PGRPs are differentially expressed in various tissues and organs: PGRP-S mainly in the bone marrow and Polymorphonuclear leukocyte (PMNs), PGRP-L mainly in the liver, and PGRP-Ia and PGRP-Ib mainly in the esophagus.
The function of only one mammalian PGRP, PGRP-S, is currently known. Mouse PGRP-S is present in neutrophils and inhibits growth of Gram-positive bacteria and, therefore, may function as a neutrophil antibacterial protein.

Supplier: AbFrontier

The p90 ribosomal S6 kinases (RSKs) comprise a family of serine/threonine kinases that lie at the terminus of the ERK pathway. In humans, the RSK family consists of four isoforms (RSK1 to -4). RSK family members are unusual among serine/threonine kinases in that they contain two distinct kinase domains, both of which are catalytically functional. Theses kinase dimains are activated in a sequential manner by a series of phosphorylations. RSK regulates gene expression via association and phosphorylation of transcriptional regulators including c-Fos, estrogen receptor, NFkappaB/IkappaB α, cAMP-response element-binding protein (CREB).
ERK activates the C-terminal kinase of RSK, leading to activation of the N-terminal kinase. Members of the RSK family are present in the cytoplasm as well as the nucleus. Addition of growth factor to the cells results in the activation of both cytosolic and nuclear RSK and the translocation of the cytosolic RSK into the nucleus upon activation. The activation and nuclear translocation of RSK result in phosphorylation and activation of transcription factors.

Supplier: AbFrontier

Transthyretin(TTR), generally called prealbumin, is a plasma protein that plays an important role in physiology such as a transporter of hormone thyroxine and retinal-binding protein. After produced primarily in the liver, TTR is excreted into the plasma. TTR represents a disproportionate fraction (25%) of CSF protein, prompting the suggestion that it is either selectively transported across the blood-CSF barrier or synthesized de novo within the central nervous system.
Transthyretin is a constituent found to the neuritic plaques, neurofibrillary tangles, and microangiopathic lesions of senile cerebral amyloid. It has been reported that more than 40 different mutations in the TTR gene associated with amyloid deposition.

Supplier: AbFrontier

The c-Jun N-terminal protein kinases (JNKs) are a family of serine/threonine protein kinases of the mitogen-activated protein kinase (MAPK) group. JNKs, which are essential regulators of physiological and pathological processes, are involved in several diseases including diabetes, atherosclerosis, stroke, and Parkinson's and Alzheimer's diseases. The JNK family consists of three isoforms; JNK1 and JNK2, which are ubiquitous, and JNK3, which is present primarily in the heart, brain and testis. Differential splicing and exon use yield 10 isoforms of JNK. JNK1 is an important mediator of insulin resistance associated with obesity, but it is also indispensable for the intact cytoarchitecture of the brain.

Supplier: AbFrontier

Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).

Supplier: AbFrontier

Coilin is a component of the nuclear Cajar(coiled) bodies (CBs) which are involved in the function or assembly/disassembly of nucleoplasmic snRNPs.
Human coilin is a 576-amino acid protein found enriched in CBs, but is also found in large amounts in the nucleoplasm.
Coilin is a constitutive phosphoprotein that is hyperphosphorylated during mitosis and it is thought that hyperphosphorylation triggers CB disassembly during cell replication. Self-interaction and localization have been shown to depend on the phosphorylation state of coilin.

Supplier: AbFrontier

Ataxia telangiectasia mutated (ATM) is a serine/threonine-specific protein kinase that is activated by DNA double-strand breaks. It phosphorylates several key proteins that initiate activation of the DNA damage checkpoint, leading to cell cycle arrest, DNA repair or apoptosis. Several of these targets are p53, CHK2, BRCA1, and H2AX.
ATM triggers the G1/S checkpoint; ATR (Ataxia telangiectasia and Rad3-related) prevents G1/S stasis. In this single point in the cell cycle, it would appear that ATM and ATR function in opposition to one another.
Ataxia telangiectasia (AT) is a rare neurodegenerative, autosomal recessive disorder characterized by chromosome instability, radiosensitivity, immunodeficiency and a predisposition for cancer.
The ATR (ATM and Rad3-related) kinase and its downstream effector kinase, Chk1, are central regulators of the replication checkpoint. Loss of these checkpoint proteins causes replication fork collapse and chromosomal rearrangements. ATR are thought to be master controllers of cell cycle checkpoint signaling pathways that are required for cell response to DNA damage and for genome stability.

Supplier: AbFrontier

Interferon alpha-2(IFNa2) which have antiviral activities, produced by macrophages. Three forms exist; alpha-2a, alpha-2b and alpha-2c.

Supplier: AbFrontier

Integrin-linked kinase (ILK) is an adaptor and signaling protein that
couples integrins to the actin cytoskeleton and coordinates signal transduction from extracellular matrix and growth factors.
By interacting with the focal adhesion proteins PINCH, paxillin, and parvin, ILK regulates integrin-mediated cell adhesion and cytoskeletal dynamics within focal adhesions to regulate cell adhesion, spreading, and migration.
ILK is involved in the suppression of apoptosis and promotion of cell survival through the phosphorylation of AKT(Ser473), GSK-3(Ser9), myosin light chain(Ser18/19), and affixin.
ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN.

Supplier: AbFrontier

Transferrin (Tf) is a blood plasma protein for iron delivery. Transferrin functions to deliver iron to cells via a receptor-mediated endocytotic process as well as to remove toxic free iron from the blood and to provide an antibacterial, low-iron environment.
Tf protein contains 679 amino acid residues and has a molecular weight of ~79 kD, having 2 specific high affinity Fe(III) binding sites. The molecule is stabilized by 19 intra-chain disulfide bonds and is protected by three carbohydrate side chains. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h).
When a Tf protein loaded with iron encounters a transferrin receptor (TfR) on the surface of a cell it binds to it and is consequently transported into the cell by endosomes. ATP-dependent proton pumps then force H+ ions into the endosomes reducing the pH to 5.5, thus promoting iron release and conformational change of the receptor enabling apo-transferrin to remain bound. The binding characteristics of the apo-Tf–TfR complex are such that the apo-Tf is released only once the complex reaches the cell surface.
Cells expressing large amounts of TfR are correspondingly competent in securing iron from Tf. Rapidly proliferating cells, as in malignancy, generally express TfR1 abundantly.
Several studies have shown a link between Tf polymorphism and susceptibility to disease. These include the rare autosomal recessive disorder atransferrinemia, cardiovascular disease (CVD) and Alzheimer’s disease.

Supplier: AbFrontier

Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

Supplier: AbFrontier

Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/ dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide–isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).

Supplier: AbFrontier

The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 – 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1).

Supplier: AbFrontier

The human Catecholamine-Sulfating Phenol Sulfotransferase (CSPS) is the only sulfotransferase that catalyses the sulfation of catecholamins, in particular the neurotransmitter dopamine, with high activity. CSPS is required for stimulation by Mn2+ of the sulfating activity and expressed in the human intestine, brain, platelet and other tissues. In the brain it may play a role in regulating the levels of dopamine. It also serves as a detoxifying function in the intestine, where it may detoxify potentially lethal dietary monoamines.

Supplier: AbFrontier

Transglutaminase(TGase) catalyses the crosslink of proteins by forming ε-(γ-glutamyl) lysine isopeptide bonds and requires the binding of Ca2+ for its activity. In mammals, eight distinct TGase isoenzymes have been identified. Tissue transglutaminase (tTGase), also known as TGase 2, has four distinct domains: N-terminal β-sandwich, catalytic core and two C-terminal β-barrel domains. tTGase may have a role in cell death, cell proliferation, cell differentiation, and receptor-mediated endocytosis. In the Alzheimer’s disease brain, the elevated tTGase activity is manifested by polymerization of a number of proteins, including Aβ peptide, β-amyloid precursor protein and the tau protein, with formation of neurofibrillary tangles.