943 Results for: "AbFrontier"

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Anti-ACTB Rabbit Polyclonal Antibody

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Human serum albumin (HSA) is the most abundant protein in mammalian plasma and is generally considered to be a multifunctional transport protein. HSA is a signle-chain protein synthesized in and secreted from liver cells. HSA has significant antioxidant activity and may represent the major and predominant circulating antioxidant in plasma, which is known to be exposed to continuous oxidative stress. HSA protects human low density lipoproteins against copper-mediated oxidation and blood against hemolysis by free radicals. HSA which are exposed to glucose and have a relatively slow turnover rate are particularly susceptible to nonenzymatic glycosylation. Structural changes in glycosylated albumin lead to a reduction in affinity for fatty acid.

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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, alpha, beta and gamma. Non Neuronal Enolase(ENO1) is an isoform of mammalian enolase and is composed of 2 alpha subunits. The gene for ENO1 also encodes a shorter monomeric structural lens protein, tau-crystallin.
Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism

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The mammalian Phospholipase C(PLC) family has two closely related proteins, PLC1 and PLC2. The PLC isozymes have the core structure domains and a unique array of domains containing an additional PH domain, two SH2 domains and one SH3 domain. In response to extracellular stimuli, such as hormones and growth factors, receptor tyrosine kinases (RTKs) phosphorylate and activate PLC. Activated PLC catalyzes hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) to produce the metabolic second messenger molecules inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG).

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Kininogens are precursors for kinin, and the two main types of them are high-molecular weight kininogen (HMWK) and low-molecular weight kininogen (LMWK). HMWK also known as the Williams-Fitzgerald-Flaujeac factor is a protein from the blood coagulation system as well as the kinin-kallikrein system. It acts mainly as a cofactor on coagulation and inflammation, and has no intrinsic catalytic activity. LMWK is produced locally by numerous tissues, and secreted together with tissue kallikrein.
Kininogens are synthesized in the liver and circulate in the plasma and other body fluids.
The kinins are pharmacologically active polypeptides released in the tissues and body fluids as a result of the enzymatic action of kallikreins on kininogens. The kinin family includes bradykinin (BK) (Arg-Pro-Pro-gly-Phe-Ser-Pro-Phe-Arg), kallidin (Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) and methionyl-lysyl-BK (Met-Lys-Arg-Pro-Pro-Gly-Phe-Arg). Kallidin and methionyl-lysyl-BK are converted into BK by aminopeptidases present in plasma and urine. Active tissue kallikrein acts on LMWK to release kallidin. The plasma kallikrein is found in circulation in an inactive form, which is known as prekallikrein or Fletcher factor.
BK and kallidin act through activation of G-protein-coupled constitutive B(2) or inducible kinin B(1) receptors linked to signaling pathways involving increased intracellular Ca concentrations and/or release of mediators including arachidonic acid metabolites, NO and EDHF (Endothelium-derived hyperpolarizing factor). In the cardiovascular system, the kallikrein-kinin system exerts a fine control of vascular smooth muscle tone and arterial blood pressure, and plays a significant cardioprotective effect.

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The epidermal growth factor receptor (EGFR) is a transmembrane receptor tyrosine kinase of the ErbB (also known as HER) family in which four members have been identified: EGFR (ErbB1), HER2/Neu (ErbB2), HER3 (ErbB3), and HER4 (ErbB4). All four erbB receptors are composed of an extracellular ligand-binding region consisting of glycosylated domains, a transmembrane domain containing a single hydrophobic anchor sequence, an intracellular region containing the catalytic tyrosine kinase domain, and a carboxyl-terminal region containing several tyrosine residues that become phosphorylated after receptor activation.
The epidermal growth factor receptor (EGFR) signaling pathway is one of the most important pathways that regulate growth, survival, proliferation, and differentiation in mammalian cells. EGFR and other members of the erbB family form either homodimers or heterodimers upon ligand binding, resulting in conformational changes that allow activation of protein kinases and transphosphorylation of key tyrosine residues within the carboxyl-terminal domain. After the induction of tyrosine phosphorylation, some signaling pathways appear to start with the recognition of the C-terminal phosphotyrosines by appropriate adaptor or signaling molecules. The aberrant activation of the EGFR leads to enhanced proliferation and other tumor-promoting activities. Several mechanisms lead to aberrant receptor activation, including receptor overexpression, gene amplification, activating mutations, overexpression of receptor ligands, and/or loss of their negative regulatory mechanisms.
The epidermal growth factor receptor (EGFR) has been extensively investigated as a target for anti-neoplastic therapy. Anti-EGFR antibodies that interfere with ligand-dependent receptor activation have shown clinical activity in a variety of solid tumors.

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IA-2 (insulinoma-associated protein 2, ICA512, PTPRN) is a member of the transmembrane protein tyrosine phosphatase (PTP) family located in secretory granules of neuroendocrine cells. The IA-2 protein is 979 amino acids in length and consists of a luminal domain, transmembrane domain, and cytoplasmic domain. Although a member of the PTP family, IA-2 lacks phosphatase activity with known substrates due to amino acid substitutions at critical sites in its PTP domain. Two paralog RPTPs, IA-2 and IA-2β were identified as major autoantigens in type-1 diabetes mellitus. On granule exocytosis, the IA-2 cytoplasmic domain is cleaved and the resulting cytosolic fragment moves into the nucleus where it enhances the levels of phosphorylated STAT5 and STAT3, thereby inducing insulin gene transcription and granule biogenesis. IA-2 signaling enhances pancreatic β–cell proliferation by regulating cyclins D through STATs.

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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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The two ubiquitin C-terminal hydrolase(UCH) enzymes, UCHL1 and UCHL3, deubiquitinate ubiquitin-protein conjugates and control the cellular balance of ubiquitin. UCHL1 and UCHL3 are both small proteins of ~220 amino acids that share more than 40% amino acid sequence identity.
UCHL3 is universally expressed in all tissues, while UCHL1 is expressed exclusively in neuronal tissue, testis and ovary. The activity of UCHL3 is more than 200 fold higher than UCHL1 when a fluorogenic ubiquitin substrate is used. UCHL1 associates with monoubiquitin and UCHL3 binds to Nedd8, ubiquitin-like protein. UCHL1 and UCHL3 play a role in the regulation of neuronal development and spermatogenesis. 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.

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The complement system is a crucial component of the innate immunity against microbial infection. Complement factor H, a 155 kDaplasma glycoprotein, is an essential regulatory protein that plays a critical role in the homeostasis of the complement system in plasma and in the protection of bystander host cells and tissues from damage by complement activation. Factor H binds to C3b, accelerates the decay of the alternative pathway C3-convertase and acts as a cofactor for the factor I-mediated proteolyticinactivation of C3b. In addition, factor H has multiple physiological activities 1) acts as an extracellularmatrix component, 2) binds to cellular receptors of the integrintype, and 3) interacts with a wide selection of ligands, such as the C-reactive protein, thrombospondin, bone sialoprotein, osteopontin, and heparin. Complement factor H has revealed an association with two different renal diseases, glomerulonephritisand atypical hemolytic uremicsyndrome (aHUS).

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Reversible phosphorylation of tyrosine residues is a key regulatory mechanism for numerous cellular events such as proliferation, differentiation, gene expression and migration. Abnormalities in tyrosine phosphorylation play a role in the pathogenesis of numerous inherited or acquired human diseases from cancer to immune deficiencies.
There are at least 107 genes coding for PTPs (protein tyrosine phosphatases) in the human genome.
All known PTPs contain a highly conserved 12 amino acid catalytic
domain and are further distinguished on the basis of additional structural motifs. The receptor-like PTPs exhibit an extracellular domain, a single transmembrane and one or two intracellular phosphatase domains. The nonreceptor cytoplasmic PTPs contain a single phosphatase domain and additional amino acid sequences that are homologous to motifs found in other classes of proteins.
Protein tyrosine phosphatases PTPN5 (STEP), PTPRR and PTPN7 comprise a family of phosphatases that specifically inactivate MAPKs (mitogen-activated protein kinases).
There are multiple forms of STEP in the adult rat brain which show differential enrichment in brain regions implicated in aspects of cognitive,
affective, and motor behaviors. Some of the STEP isoforms are generated through alternative splicing of a single STEP gene and each has unique intracellular targets and functions.

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Anti-mRNA capping enzyme Mouse Monoclonal Antibody [clone: T16-AF3F1]

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Mitogen- and stress-activated protein kinases (MSK2) is nuclear kinase that act downstream of mitogen-activated protein/extracellular signal-regulated kinase pathways. It contains two kinase domains in the N-terminal and C-terminal region, respectively. MSK2 is activated in response to mitogenic stimuli via Erk1/2MAPK pathway and also by stress stimuli via p38MAPK pathway. Signals from mitogens and cellular stresses are involved in many functions including cell proliferation, differentiation, and survival through the phosphorylation of cyclic AMP response element-binding protein (CREB) at Ser133 which is catalyzed by MSK2. Recently, MSK2 has been shown to be required for stress-induced phosphorylation of histone H3-Ser and transcriptional activation of several immediate early genes.

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Cyclin-dependent kinase-5(CDK5) is a member of the cyclin-dependent kinase family of serine/threonine kinases. Its mRNA and protein are expressed in the kidneys, testes, and ovaries. And Its activity has been detected almost exclusively in brain extracts.
Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity; however, Cdk5 is not activated by cyclins. Instead, Cdk5 activity requires association with one of two brain-specific regulatory subunits, called p35 and p39. These two activators regulate the spatial and temporal expression of active Cdk5, restricting its activity primarily to post-mitotic neurons.

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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.
Human complement factor C6 is one of five components (C5b, C6, C7, C8, and C9) that interact to form the cytolytic membrane attack complex (MAC) which is the cytolytic end product of the complement cascade. MAC is typically formed on the surface of intruding pathogenic bacterial as a result of the activation of the complement system, and it is one of the ultimate weapons of the immune system.
The sixth component of complement, C6, is a 913 amino acid single polypeptide chain serum glycoprotein. Homology study suggests that C6 could contain two domains, an amino-terminal region that is related to complement C8 and C9, and a carboxyl-terminal region that has partial homology to the complement regulatory proteins factor H and factor I.
Genetic deficiencies of terminal complement components lead to markedly increased susceptibility to only one particular Gram-negative genus, the Neisseria. The susceptibility is attributable to the major role played by complement-mediated killing in host defense against the pathogen.

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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.

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Cyclins play a key role in the orderly progression of the cell division cycle through their timed expression and their ability to bind, activate and enhance substrate affinity of their associated cyclin-dependent protein kinases (CDKs). E-type cyclins (cyclin E1 and cyclin E2) are expressed during the late G1 phase of the cell cycle until the end of the S-phase. Cyclin E binds and activates the kinase Cdk2 and by phosphorylating its substrates, the cyclic/Cdk2 complexes initiate a cascade of events that leads to the expression of S-phase specific genes. Besides this specific function as a regulator of S-phase-entry, cyclin E plays a direct role in the initiation of DNA replication, the control of genomic stability, and the centrosome cycle.

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Signal transducer and activator of transcription (STAT), named after their dual role, generally mediate cytokine, growth factor and hormone receptor signal transduction. In mammals, seven STAT proteins have been identified. STAT5 has been implicated in cellular functions of proliferation, differentiation and apoptosis with relevance to processes of hematopoiesis and immunoregulation, reproduction, and lipid metabolism. Two highly homologous STAT5 isoforms, 96kDa STAT5a and 94kDa STAT5b, are encoded by two tandemly linked genes. Although both STAT5 isoforms are roughly 95% homologous at the level of cDNA, they exhibit both redundant and non-redundant functions in vivo, probably due to differences in their transactivation domain. Aberrant regulation of STAT5 has been observed in solid tumors as well as in patients with either chronic or acute myeloid leukemia. Kinase inhibitors are currently being developed to negatively regulate STAT5 activity for clinical purposes.

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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 RelB protein is present in the cytosol, bound to p50 or p52 and an inhibitory IκB protein, forming an inactive trimeric complex. Following cell signalling events leading to IκB degradation, Rel/NFκ-B proteins are translocated to the nucleus where they regulate gene expression. The genes controlled by Rel/NF-κB family members are predominantly genes involved in the host response to infection, stress and injury. RelB mediates the regulation of genes involved in immune and inflammatory processes.

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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-bisphos-phoglycerate 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 (1), DNA repair (2), nuclear RNA export (3-4), membrane fusion (5) 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 (6-7).

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There are ten mitogen-activated protein kinase (MAPK) phosphatases (MKPs) that act as negative regulators of MAPK activity in mammalian cells.
MKP2(DUSP4) is a dual threonine/tyrosine phosphatase that specifically dephosphorylates and inactivates MAPKs(ERK, JNK, p38). It contains one Rhodanese domain and one tyrosine-protein phosphatase domain.
MKP2 is expressed in a variety of tissues, and is localized in the nucleus.
Transcription factor E2F-1 acts as a transcriptional regulator of MKP2. E2F-1/MKP2 pathway mediates apoptosis under oxidative stress and that MKP2 suppresses tumor formation.
MKP2 is a novel transcription target of p53 in mediating apoptosis by 10-bp palindrome motif (CTGGCGCCAG) in the MKP2 promoter.

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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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Catalase is a homotetrameric heme-containing enzyme present within the matrix of all peroxisomes. It carries out a dismutation reaction in which hydrogen peroxide is converted to water and oxygen. Human catalase has the last four amino acids (-KANL) at the extreme C-terminus for peroxisome targeting. The monomer of human catalase is 61.3 kD in molecular size. Catalase has been implicated as an important factor in inflammation, mutagenesis, prevention of apoptosis, and stimulation of a wide spectrum of tumors. Loss of catalase leads to the human genetic disease, acatalasemia, or Takahara’s disease (1).

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The inter-α-trypsin inhibitor (ITI, IαI) family, a typical and classical example for protein-glycosaminoglycan-protein (PGP) complexes, occurs constitutively in plasma at relatively high concentrations and is a result of alternate combinations of three kinds of heavy chains with a common light chain, the bikunin proteoglycan. Bikunin has two proteinase inhibitor domains and belongs to the Kunitz-type protease inhibitor family; it displays an inhibitory activity against trypsin, leukocyte elastase and plasmin. The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid and this binding promotes the stability of the extra-cellular matrix. The ITI protein family is suspected of playing a key role in the extra-cellular matrix biology.

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Plasmid vectors for the expression of coding regions of eukaryotic genes in bacterial, insect and mammalian hosts are in common usage. The expression vectors are used to encode hybrid fusion proteins consisting of a eukaryotic target protein and a specialized region designed to aid in the
purification and visualization of the target protein. Short pieces of welldefined peptides(Poly-His, Flag-epitope or cmyc epitope or HA-tag) or small proteins (bacterial GST, MBP) is often cloned along with the target gene. The HA tag is derived from an epitope of the influenza hemagglutinin protein, which has been extensively used as a general epitope tag in expression vectors. It has been successfully used in a
variety of applications, including Western blotting, Immunoprecipitation, and immunofluorescence studies.

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Synuclein is a small, soluble protein primarily expressed in neural tissue. The synuclein family includes three known proteins: α-synuclein, β-synuclein, and γ-synuclein.
α-Synuclein is a very conserved, small acidic protein (140 residues) with a molecular weight of approximately 19 kDa that accounts for about 1% of total protein in neurons. It is concentrated primarily in presynaptic axon terminals and plays a central role in initiating Parkinson’s disease. It is the principal constituent of Lewy bodies which are formed by protein aggregation and inclusion body formation.
α-Synuclein lacks secondary or tertiary structure, so it belongs to the family of natively unfolded proteins, many of which act as chaperones. Much of this α-synuclein has been post-translationally modified to increase the rate of oligomerization.
Mutant forms of α-Synuclein are associated with autosomal dominant Parkinson’s disease. The mutations increase the aggregation rate of the resultant α-synuclein
β-Synuclein is found primarily in brain tissue and is seen mainly in presynaptic terminals. It is predominantly expressed in the neocortex, hippocampus, striatum, thalamus, and cerebellum.
β-Synuclein may protect the central nervous system from the neurotoxic effects of α-synuclein by inhibiting aggregation of α-synuclein which occurs in neurodegenerative diseases such as Parkinson's disease.
γ-Synuclein is a synuclein protein found primarily in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. γ-Synuclein expression in breast tumors is a marker for tumor progression.

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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 (alpha, beta, and gamma), novel PKCs (Delta, Epsilon, Eta, and IPA), and atypical PKCs (Zeta and Lambda/Iota). PKC Gamma is a member of the cPKC subfamily which is activated by Ca2+ and diacylglycerol in the presence of phosphatidylserine. Physiologically, PKC Gamma is activated by a mechanism coupled with receptor-mediated breakdown of inositol phospholipid as other cPKC isotypes. PKC Gamma is expressed solely in the brain and spinal cord and its localization is restricted to neurons. Within the brain, PKC Gamma is the most abundant in the cerebellum, hippocampus and cerebral cortex, where the existence of neuronal plasticity has been demonstrated.

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α-1-antichymotrypsin (ACT) is a glycoprotein with a molecular weight of 55~68 kDa and 25% by weight of various sugars, whose heterogeneity results in variation of molecular weight. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. Plasma ACT levels might increase rapidly more than 5-fold during an acute phase reaction, ACT has been shown to promote Aβ polymerization in vitro and in vivo, and levels of ACT protein in plasma and cerebrospinal fluid from Alzheimer's patients have been found to correlate with progression of dementia.

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Cyclin-dependent kinase-5(CDK5) is a member of the cyclin-dependent kinase family of serine/threonine kinases. Its mRNA and protein are expressed in the kidneys, testes, and ovaries. And Its activity has been detected almost exclusively in brain extracts. Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity; however, Cdk5 is not activated by cyclins. Instead, Cdk5 activity requires association with one of two brain-specific regulatory subunits, called p35 and p39. These two activators regulate the spatial and temporal expression of active Cdk5, restricting its activity primarily to post-mitotic neurons.

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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.