743 Results for: "ABFRONTIER"

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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).

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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).

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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.

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Glutamine Synthetase(GS) catalyzes the conversion of ammonia and glutamate to glutamine. This reaction consumes a molecule of ATP:
Glutamate + NH4+ + ATP
 Glutamine + ADP + Pi
GS is found in astrocytes as an octamer of identical 45kDa subunits. Most well known function of GS is the detoxification of brain ammonia. It also has an important role in controlling metabolic regulations of neurotransmitter glutamate. Because of the multiple functions and importance of GS in cellular metabolism, both catalytic activities and synthesis are highly regulated. The activity of GS is controlled by adenylylation. Its activity is decreased in the cerebral cortex of brains affected by Alzheimer’s disease, particularly in the vicinity of senile plaques. It is also decreased under conditions of glucose deprivation. On the other hands, the level of expression of GS is increased during ischemia in vivo or hypoxia in culture.

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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 thioredoxindependent 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.

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Antithrombin III is a plasma protein synthesized in the liver and has molecular weight of 58kDa. Antithrombin III is a heparin-binding glycoprotein that acts as the major inhibitor of thrombin. Also it interferes with several plasma proteases, including kallikrein and factors IXa, Xa, XIa and XIIa, thereby playing a central role in regulating coagulation. It is also used as a therapeutic agent in patients with sepsis and disseminated intravascular coagulation. In addition, a number of recent studies have shown that antithrombin III has anti-inflammatory properties, which are independent of its effects on coagulation.

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Anti-PRDX-SO3 Mouse Monoclonal Antibody [clone: 10A1]

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The Heat shock protein 70(HSP70) family was found in many intracellular compartments. Members of this protein occur in chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variety of biological stresses, including heat stress, in every organism. HSP70 serves a variety of roles: 1) It acts as molecular chaperones facilitating the assembly of multi-protein complexes, 2) It participates in the translocation of polypeptides across cell membranes and to the nucleus 3) It aids in the proper folding of nascent polypeptide chains. HSP70 is mitochondrial import machinery and plays key roles in the cytosolic endoplasmic reticulum. Recently, extracellular localized HSP have been found to play key roles in the induction of a cellular immune response.

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Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). Mitochondrial membrane permeabilization and subsequent release of apoptotic factors are key mechanisms during this process.
The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4).
Bid consists of only one Bcl-2 homology domain, BH3. Bid cleavage to tBid (truncated Bid) activates apoptotic pathway at the mitochondrial level. Cleavage of cytosolic Bid and subsequent mitochondrial translocation have been detected in neuronal cell death related to acute or chronic neurodegeneration. Pharmacological inhibition of Bid can be a promising therapeutic strategy in neurological diseases where programmed cell death is prominent.
After Bid activation and mitochondrial translocation, the most prominent downstream mechanisms of Bid-dependent neuronal apoptosis involve disruption of mitochondrial membrane integrity and intracellular calcium homoeostasis and the release of pro-apoptotic mitochondrial factors such as cytochrome c.

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Protein Phosphatase 2A (PP2A) is a ubiquitous and conserved Serine/Threonine phosphatase and accounts for a large fraction of phosphatase activity in eukaryotic cells. PP2A plays an important role in cell cycle regulation, cell growth control, development, regulation of various signal transduction pathways, and cell mobility.
PP2A comprises A and B subunits which are regulatory and a catalytic C subunit. When the PP2A catalytic C subunit (36 kDa) associates with the regulatory A (65 kDa, PR65) and B subunits (PR55, PR56, PR72, PR93 etc), wide variety of heterotrimeric holoenzymes are produced with distinct functions and characteristics. The different association of the subunits give PP2A large regulatory flexibility and differential substrate specificity. The A subunit exists as two isoforms ( α and β ) as does the C subunit, whereas the B subunits fall into three families designated B, B' (also called B56), and B''. The A subunit is the scaffold required for the formation of the heterotrimeric complex and the binding of A subunit alters the enzymatic activity of the catalytic subunit, even if the B subunit is absent.

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α1-Microglobulin (protein HC) is a lipocalin with immunosuppressive properties. The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids. Well known lipocalins are α1-microglobulin, α-1-acid glycoprotein (orosomucoid), apolipoprotein D, β-lactoglobulin, and complement component C8 γ chain etc. A gene in the lipocalin cluster encodes α1-microglobulin together with a Kunitz-type proteinase inhibitor, bikunin. The gene is translated into the α1-microglobulin-bikunin precursor, which is subsequently cleaved and the two proteins secreted to the blood separately.
α1-Microglobulin, is a monomeric protein of a molecular size of 27 kDa. It is produced by the liver and circulates in a free form, but is also bound in complexes to high molecular weight molecules. In human plasma, approx. 50% of α1-microglobulin forms a one-to-one complex with monomeric immunoglobulin A (IgA) by a reduction resistant bond.
Normal urine contains very small amounts of α1-microglobulin. In conditions with disturbed tubular function, reabsorption of α1-microglobulin is reduced and increased amounts are found in urine. Urinary α1-microglobulin seems a promising marker for renal abnormalities and for the differentiation of various nephrological and urological pathologies.

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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).

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The MAP Kinase pathway is a key signaling mechanism that regulates many cellular functions such as cell growth, proliferation, differentiation, development, transformation and apoptosis. The basic arrangement includes a G-protein, a MAPK kinase kinase (MAPKKK) that phosphorylates and activates a MAPK kinase (MAPKK), which in turn phosphorylates MAPK. The ERK (extracellular-signal regulated kinase) cascade is a central MAPK pathway which contains Ras as a G protein, Raf as a MAPKKK, MEK1 (MAPK/ERK kinase1) and MEK2 (MAPK/ERK kinase2) as MAPKK, and ERKs as MAPK. MEK1 and MEK2 are  80% identical to each other, and are essentially identical in most of their kinase domain. MEK1 and MEK2 phosphorylate ERKs equally well, both in vivo and in vitro. MEK1 (45 KDa) and MEK2 (46 KDa) are composed of a catalytic kinase domain, which is surrounded by a regulatory N-terminal domain ( 80 amino acids) and a shorter C-terminal region ( 30 amino acids). Unlike the kinase domains, the N-termini and the characteristic Pro-rich inserts are quite divergent between the two MEKs (40% identity). MEKs are activated by phosphorylation of two Ser residues in their activation loop (Ser218 and Ser222 in MEK1) located within a Ser–Xaa–Ala–Xaa–Ser/Thr motif, typical to all MAPKKs.

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Ubiquitin(Ub) is a small protein that is composed of 76 amino acids. Ub is found only in eukaryotic organisms and is highly conserved. Ub can exist either in free form or as part of a complex with other proteins. In the latter case, Ub is attached(conjugated) to proteins through a covalent bond between the glycine at the C-terminal end of Ub and the side chains of lysine on the proteins; Ubiquitination.  Ub functions to regulate protein turnover in a cell by closely regulating the degradation of specific proteins. Ubiquitin has been immunohistochemically localized to a number of pathological inclusions, including ; Lewy bodies of Parkinson’s disease,neurofibrillary of Alzheimer’s disease, Pick bodies of Pick’s disease.

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The complement system is a part of the larger immune system and three biochemical pathways are present: the classical complement pathway, the alternative pathway, and the mannose-binding lectin pathway.
Complement component C4 is an essential component of humoral immune response. In its activated form, C4b becomes a subunit of the C3 convertase, which is an enzymatic complex that activates C3 of the classical and lectin complement activation pathways. The classical pathway is initiated by the activation of the C1-complex (C1q, C1r and C1s) by C1q's binding to antibody-antigen. The C1-complex now binds to and splits C2 and C4 producing C2a and C4b. C4b and C2a bind to form C3-convertase. Production of C3-convertase leads to cleavage of C3 into C3a and C3b and C3b joins with the C3 convertase to make C5 convertase.
Human C4 is the most polymorphic protein of the complement system. Complement C4 exists as two isotypes, C4A (acidic) and C4B (basic). Although the sequence identity is very high, they have different hemolytic activities, covalent affinities to antigens and immune complexes, and serological reactivities. Each C4 contains β chain, α chain, C4a anaphyltoxin, C4b, and γ chain.
C4-deficient mice shows incomplete clearance of microbial attack and C4-deficiency in human shows increased autoimmune diseases.

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α-1-B glycoprotein (A1BG) which is a plasma protein with no known function belongs to the immunoglobulin superfamily. Although the human A1BG has been known for four decades, and the information about the amino acid sequence, chromosomal assignment, and even genetic polymorphism in different populations have been known, no biological function has been suggested. A1BG (Mr approximately equal to 63,000) consists of one polypeptide chain of 474 amino acids with four glucosamine oligosaccharides. The polypeptide has five intrachain disulfide bonds and consists of five repeating structural domains, each containing about 95 amino acids and one disulfide bond.
Recently human cyctein-rich secretory protein 3 (CRISP-3) has been found to be a binding partner of A1B, suggesting the A1BG-CRISP-3 complex displays a protecting function from a potentially harmful effect of free CRISP-3 in circulation.

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α2-Macroglobulin (α2M), is a 720-kDa homotetrameric glycoprotein composed of four identical 180 kDa subunit. α2M shares with other α-macroglobulins, like the complement components C3 and C4 and the pregnancy zone protein PZP, an extraordinary binding capacity for a variety of ligands. This allows the α-macroglobulins to serve as humoral defense barriers against foreign peptides in the plasma. α2M interacts and captures virtually any proteinase, often referred to as a panprotease inhibitor. In the brain of Alzheimer's disease (AD) patients, α2M also has been localized to diffuse amyloid plaques, supporting an important role for α2M in AD etiopathology.

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Human Complement C3 (C3) is synthesized as a single-chain pro-molecule (185 kDa) that then suffers several post-translational modifications. Before being secreted as a mature protein, C3 is split into -chain (645 residues and 70 kDa) and  chain (992 residues and 115 kDa) and forms a rare internal thioester bond. C3 plays a central role in the activation of all the three pathways of complement activation i.e. the classical, alternative, and lectin pathway. As C3 is the major complement component and participates in several stages of the immune response, its deficiency generally associated with higher susceptibility to severe bacterial infections and in some cases with autoimmune diseases such as systemic lupus erythematosus.

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Fibrinogen is a soluble glycoprotein found in the plasma, with a molecular weight of 340kDa. It comprises of three pairs of non-identical polypeptide chains (α, 63.5kDa β, 56kDa, and γ, 47kDa chains) linked to each other by disulphide bonds. Low plasma fibrinogen concentrations are therefore associated with an increased risk of bleeding due to impaired primary and secondary hemostasis. Therefore Fibrinogen is an essential component of the blood coagulation system. Also it may play key roles in the process of atherosclerotic lesion formation, with subsequent effects on cardiovascular diseases. And increasing evidence from epidemiological studies suggests that elevated plasma fibrinogen levels are associated with an increased risk of ischaemic heart disease(IHD), stroke and other thromboembolism.

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Myeloperoxidase is a major neutrophil protein and is also present in monocytes. In neutrophils, it is stored in azurophilic granules and released during phagocytosis. It is a heme enzyme that uses the superoxide and hydrogen peroxide generated by the neutrophil oxidative burst to produce hypochlorous acid and other reactive oxidants.The produced hypochlorous acid reacts with and destroys bacteria. In many inflammatory pathologies, such as cystic fibrosis and rheumatoid arthritis, neutrophils are also causing tissue damage. MPO is thought to be the most promising cardiac marker at the moment. In addition to that MPO is a good inflammatory biomarker for autoimmune, inflammatory diseases and cancer.

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Kallikreins(KLKs) belong to the serine protease family of proteolytic enzymes. Neurosin(KLK6), one of these, is atrypsin-like protease dominantly expressed in the human brain but also in a variety of other tissues. As measured by a sensitive quantitative assay in serum and cerebrospinal fluid(CSF), it may have value as a biomarker for diagnosis and monitoring of Alzheimer's disease(AD). It seems to be down regulated in serum and tissues of AD patients and may be involved in amyloid metabolism.

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Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

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Protein kinase C (PKC) is a family of serine-threonine kinases that regulate a broad spectrum of cellular functions. The family is composed of nine genes that express structurally related phospholipid-dependent kinases with distinct means of regulation and tissue distribution. Based on their structures and sensitivities to Ca2+ and diacylglycerol (DAG), they have been classified into conventional PKCs (α, β, and γ), novel PKCs (δ, ε, η, and θ), and atypical PKCs (ζ and λ/ι).
Mammalian PKC α consists of 672 amino acids and is distributed in all tissues, in contrast to other PKC isotypes whose expression is restricted in the particular tissues. PKC α is activated by a variety of stimuli originating from receptor activation, cell contact and physical stresses. Kinase activity of PKC α is regulated by phosphorylation of three conserved residues in its kinase domain: the activation-loop site Thr-497, the autophosphorylation site Thr-638, and the hydrophobic C-terminal site Ser-657. In some types of cells, PKC α is implicated in cell growth, in contrast, it may play a role in cell cycle arrest and differentiation in other types of cells. The responses are modulated by dynamic interactions with cell-type specific factors.

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Methionine sulfoxide reductase (MsrA) reduces methionine sulfoxide (MetO) residues in proteins and free MetO to Methionine (Met). The catalytic activity of MsrA is dependent of bound metal and cofactors but it requires reducing equivalents from either DTT or a thioredoxin-regenerating system. MsrA plays an essential role in protecting cells against oxidative damage. The substrates of MsrA include calmodulin, HIV protease and 1-proteinase-inhibitor (1-3). Recent studies indicate that there is a connection between MsrA and Alzheimer’s disease in mammals (4).

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14-3-3, a family of acidic and soluble proteins, highly conserved in amino acid sequences from yeast to mammals, is expressed in all eukaryotic cells. Seven isoforms(β, γ, ε, η, ζ, σ and τ/θ) encoded by seven distinct genes are identified in mammals and forms homo- and hetero- dimeric cup-shaped structures. As 14-3-3 is interacted with more than 100 binding partners, it regulates key proteins involved in various biological processes such as signal trans-duction, cell cycle, transcriptional control, cell proliferation, apoptosis, and ion channel physiology. Most 14-3-3 requires phosphorylation of serine or threonine residues in the target sequence. This protein is abundantly expressed in the brain and has been detected in the cerebrospinal fluid of patients with different neurological disorders.

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Protein kinase C (PKC) is a family of serine-threonine kinases that regulate a broad spectrum of cellular functions such as cell migration and polarity, proliferation, differentiation, and cell death. The family is composed of several genes that express structurally related phospholipid-dependent kinases with distinct means of regulation and tissue distribution. Based on their structures and sensitivities to Ca2+ and diacylglycerol (DAG), they have been classified into conventional PKCs (α, β, and γ), novel PKCs (δ, ε, η, and θ), and atypical PKCs (ζ and λ/ι). PKCs share a structural backbone, mainly consisting of a regulatory domain at the N-terminus and a catalytic domain at the C-terminus. All family members require phosphatidylserine, a component of the phospholipid bilayer, for their activation.
Some PKCs (PKCα, δ, and ζ) are widely expressed in all tissues, but other isoforms are expressed in a tissue-specific manner. PKCγ, for example, is largely confined to brain and neuronal tissue, PKCι is mainly expressed in testis and insulin secreting cells, and PKCθ is mainly expressed in skeletal muscle.
PKC epsilon (PKCε) is a calcium-independent and phorbolester/diacylglycerol-sensitive serine/threonine kinase. PKCε is the only PKC isozyme that has been shown to behave as an oncoprotein. Constitutive activation of PKCε in a small cell lung cancer (SCLC) cell line and the overexpression of PKCε in colonic epithelial cells have been reported.

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Anti-G-CSF Rabbit Polyclonal Antibody

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The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. 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).

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Vimentin is a member of the intermediate filament family of proteins found in various non-epithelial cells, especially mesenchymal cells. Vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol. Although most intermediate filaments are stable structures, vimentin also has a dynamic nature which is important when offering flexibility to the cell.
Two monomers which have central α-helical domains, capped on each end by non-helical domains twist around each other to form a coiled-coil dimer. Two dimers then form a tetramer, which, in turn, form a sheet by interacting with other tetramers.
There are some reports related to the biochemical function of intermediate filament network. The intracellular movement of LDL-derived cholesterol from the lysosome to the site of esterification is a vimentin-dependent process. A role for vimentin in mechanotransduction of shear stress has also been suggested. The mechanical stress of fluid shear on endothelial cells seems to trigger MAPK signaling pathways and stimulates proliferation.

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Anti-CTSH Mouse Monoclonal Antibody [clone: AF14D7]