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The Notch signaling pathway is important for cell-cell communication, which involve gene regulation mechanisms that control multiple cell differentiation processes during embryonic and adult life. It critically influences cell proliferation, differentiation, and apoptosis in metazoans. The hairy and enhancer of split (HES) family is a basic helix-loop-helix (bHLH) type trancriptional repressor and acts as Notch effectors by negatively regulating expression of downstream target genes such as tissue-specific transcription factors. HES-1 is an upstream negative regulator of REST expression. Silencing of the transcriptional repressor REST is required for terminal differentiation of neuronal and β-cells.
Recent integrative genomic analyses on HES/HEY family suggest that HES1 and HES3 are target genes of the embryonic stem cell-specific network of transcription factors, and that HES1, HES5, HEY1, HEY2 and HEYL are target genes of Notch signaling pathway.

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Shc is a prototype adapter protein that is expressed from the earliest stages of T-cell development. Shc becomes rapidly tyrosine phosphorylated after T-cell receptor (TCR) engagement.
Three shc genes have been identified in mammals and their gene products have been referred to as ShcA, ShcB and ShcC. ShcA is ubiquitously expressed, while shcB and ShcC expression appear limited to neuronal cells. ShcA is expressed as three isoforms of about 46, 52 and 66 kDa.
Shc is composed of an N-terminal PTB, a central collagen-homology (CH) domain and a C-terminal SH2 domain. The 66 kDa isoform of ShcA is expressed in most cells except in the hematopoietic lineage and contains an additional amino-terminal CH-like region.
The tyrosine phosphorylation of Shc has been noticed upon engagement of numerous cell surface receptors such as growth factor receptors, antigen receptors, cytokine receptors, G-protein coupled receptors and hormone receptors. The involvement of ShcA in the Ras signaling pathway is initiated by the tyrosine-phosphorylation of the receptor protein tyrosine kinases (RPTKs) and subsequent interaction with Grb2 and Ras guanine nucleotide exchange factor, Sos. The Shc : Grb2 : Sos complex gets localized to the membrane through the interaction of Shc with the phosphorylated receptor. Membrane-bound Sos then activates Ras by catalysing GDP/GTD exchange. GTP-bound Ras then triggers downstream events, which include Raf, the mitogen-activated protein kinases (MAPKs) and MAPK kinase (MEK).

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The members of the Src-family kinases are Src, Lyn, Fyn, Yes, Hck, Lck, Fgr, Blk, and Yrk. Each of these have a common structure consisting of an unique domain at the N-terminal, followed by SH3, SH2 and tyrosine kinase domains.
In immume cells, the Src-family kinases play roles as critical regulators of a large number of intracellular signaling pathways, including integrin signaling pathway. Integrins are major cellular receptor that mediate cell to cell and cell to substratum interactions.
Lck is expressed almost exclusively in T cells and interacts with cytoplasmic regions of CD4 and CD8 coreceptor molecules, and thus plays an important role in relaying TCR-mediated activation signal. Lck is
regulated by phosphorylation of its Tyr394 and Tyr505.

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Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes.
Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels.
Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is
regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios.
The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay.

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ROCK, Rho-associated coiled-coil forming kinases, is a protein serine/threonine kinase that is activated when bound to the GTP-bound form of Rho. The small GTPase Rho regulates formation of focal adhesions and stress fibers of fibroblasts, as well as adhesion and aggregation of platelets and lymphocytes by shuttling between the inactive GDP-bound form and the active GTP-bound form. Rho is also essential in cytokinesis and plays a role in transcriptional activation by serum response factor. ROCK, as a downstream effector of Rho, phosphorylates and activates LIM kinase, which in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. ROCK2 regulates cytokinesis, smooth muscle contraction, the formation of actin stress fibers and focal adhesions, and the activation of the c-fos serum response element.

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TRBP (transactivation response RNA binding protein) is a protein that increases HIV-1 expression and replication by inhibition of the interferon-induced protein kinase PKR. TRBP overexpression is associated with reduced abundance of phosphorylated PKR and stimulation of protein translation.
TRBP has a physiological role in spermatogenesis and growth control during development. It is oncogenic upon overexpression, likely because of its association with PKR, with the PKR activator PACT, and with the tumor suppressor Merlin. TRBP was identified as a merlin interacting protein by Gal4-based yeast two-hybrid screening of a human adult brain cDNA library. Merlin can inhibit tumorigenesis mediated by TRBP and can regulate the protein translation pathways controlled by TRBP.
Dicer is a key enzyme involved in RNA interference (RNAi) and microRNA (miRNA) pathways. Ago-2, a member of the Argonaute family, Dicer and TRBP comprise the catalytic core of the RNA induced silencing complex (RISC).

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The casein kinase I (CKI) family of serine/threonine protein kinases is highly conserved from yeast to humans. The CKI family is involved in many diverse and important cellular functions, such as regulation of membrane transport, cell division, DNA repair, circadian rhythms, and nuclear localization.
The name of the enzyme family was originated from the convenience of casein as a substrate since the earliest days of research on protein phosphorylation.
Casein kinase 2 (CK2) is a ubiquitous, highly conserved, essential serine/threonine kinase which has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes.
CK2 is a tetramer of two α subunits and two β subunits. The α subunits have the catalytic kinase domain. Loss of the α‘ catalytic subunit produces male infertility, and loss of the single β regulatory subunit is
early embryonic lethal.
CK2 appears to be upregulated in most cancers and the promotion of tumorigenesis by the overexpression of CK2 has been reported in transgenic mice.

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Vitronectin is an 75 kDa glycoprotein consisting of 459 amino acid residues. It is abundant in blood plasma and the extracellular matrix. Vitronectin contains three glycosylation sites that contribute approximately 30% of its molecular mass. It circulates as a single-chain (75 kDa) and two-chain (10 and 65 kDa) forms under reducing conditions. Under non-reducing conditions, the N-terminal 65 kDa and C-terminal 10 kDa fragments are linked by a single disulfide bond .
Vitronectin has been implicated as a regulator of many diverse physiological processes including coagulation, fibrinolysis, pericellular proteolysis, complement dependent immune response, cell attachment and spreading. Cell adhesion and migration are directly involved in cancer metastasis and tumor malignancy.
The Somatomedin B domain of Vitronectin binds to Plasminogen activator inhibitor-1 (PAI-1), and stabilizes it. Thus vitronectin serves to regulate proteolysis initiated by plasminogen activation. Additionally vitronectin is a component of platelets and is thus involved in hemostasis via heparin binding which neutralizing antithrombin III inhibition of thrombin and factor Xa. Vitronectin contains an RGD (45-47) sequence which is a binding site for membrane bound integrins, which serve to anchor cells to the extracellular matrix.

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The Rb protein (pRb, 110kDa) is a tumor suppressor, which plays a pivotal role in the negative control of the cell cycle and in tumor progression. pRb is responsible for a major G1 checkpoint, blocking S-phase entry and cell growth. pRb prevents the cell from replicating damaged DNA by preventing its progression through the cell cycle into its S phase or progressing through G1 phase. pRb can actively inhibit cell cycle progression when it is dephosphorylated while this function is inactivated when pRb is phosphorylated. pRb is activated near the end of mitosis (M phase) when a phosphatase dephosphorylates it, allowing it to bind E2F. The pRb protein represses gene transcription, required for transition from G1 to S phase, by directly binding to the transactivation domain of E2F and by binding to the promoter of these genes as a complex with E2F.

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The casein kinase I (CKI) family of serine/threonine protein kinases is highly conserved from yeast to humans. The CKI family is involved in many diverse and important cellular functions, such as regulation of membrane transport, cell division, DNA repair, circadian rhythms, and nuclear localization.
The name of the enzyme family was originated from the convenience of casein as a substrate since the earliest days of research on protein phosphorylation.
Casein kinase 2 (CK2) is a ubiquitous, highly conserved, essential serine/threonine kinase which has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes.
CK2 is a tetramer of two α subunits and two β subunits. The α subunits have the catalytic kinase domain. Loss of the α‘ catalytic subunit produces male infertility, and loss of the single β regulatory subunit is
early embryonic lethal.
CK2 appears to be upregulated in most cancers and the promotion of tumorigenesis by the overexpression of CK2 has been reported in transgenic mice.

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Anti-NF2 Mouse Monoclonal Antibody [clone: AF1G4]

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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. RelA(p65) subunit of NF-κB is a crucial regulator of apoptosis. RelA subunit mediates resistance to programmed cell death induced by many stimuli, including TNF, chemotherapy agents and ionizing radiation, through inducing the expression of a wide variety of anti-apoptotic genes.

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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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Epitope tags can be used to label and detect proteins with immunoblotting, immunoprecipitation and immunostaining techniques.
Due to their small size, they are unlikely to affect the tagged proteina's biochemical properties. The Myc epitope tag is widely used to detect
expression of recombinant proteins in bacteria, yeast, insect and mammalian cell systems. Myc proteins are nuclear proteins with relatively
short half-lives. Amplification of the c-Myc gene has been found in several types of human tumors including lung, breast and colon carcinomas.

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Anti-IRAK4 Rabbit Polyclonal Antibody

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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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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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Diazepam Binding Inhibitor(DBI) is a highly conserved 10 kDa polypeptide which is expressed in various species range from yeast to mammals. As an inverse agonist for benzodiazepine receptors, DBI downregulates inhibitory effects of GABA. It also has potential to induce anxiety. Found in central and peripheral tissues, DBI also participates in metabolism of steroids, which has been known to partially modify GABAA receptor function in the CNS. In peripheral tissues, DBI plays regulatory roles in steroidogenesis. DBI levels have been reported to be decreased in the cerebrospinal fluid obtained from patients with Alzheimer disease.

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α-1-Acid glycoprotein (AGP) is a protein with a molecular weight of 41~43 kDa and is heavily glycosylated (45%). Due to the presence of sialic acids, it is negatively charged (pI=2.7-3.2). AGP is one of the major acute phase proteins in humans. As most acute phase proteins, its serum concentration increases in response to systemic tissue injury, inflammation or infection, and these changes in serum protein concentrations have been correlated with increases in hepatic synthesis. Also, its glycosylation pattern can change depending on the type of inflammation. The biological function of AGP remains unknown; however, AGP is believed to regulate the interaction between blood cells and endothelial cells, and regulates the extravasation of the cells during infection and inflammation.

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Hematopoietic progenitor kinase 1 (HPK1) is a 97 kDa serine/threonine protein kinase expressed only in hematopoietic cells and tissues. HPK1 is comprosed of a STE20-like kinase domain in its N-terminus, four proline-rich motifs (-P-x-x-P-), a caspase cleavage site, and a distal C-terminal Citron homology domain. The proline-rich motifs are capable of binding proteins that contain SH3 domains.
HPK1 is involved in many cellular signaling cascades that include MAPK signaling, antigen receptor signaling, apoptosis, growth factor signaling, and cytokine signaling. HPK1 binds many adaptor proteins including members of the Grb2 family, Nck family, Crk family, SLP-76 family, and actin-binding adaptors. HPK1 contains 13 potential tyrosine phosphorylation residues, some of which may be phosphorylated by ZAP-70, which provide potential docking sites for SH2 domains containing proteins.
HPK1 is activated by both EGF and PDGF stimulation where adaptor proteins are involved in mediating the localization of effector molecules to cell surface receptors.
Activation-induced cell death (AICD)-resistant T cells contain full-length HPK1, while AICD-sensitive T cells have HPK1-C (cleaved form). HPK1 might be a possible molecular switch used to discriminate between the extrinsic pathway involving death receptors and the intrinsic pathway determined by the ratio between anti- and pro-apoptotic Bcl-2 family members.

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Voltage-dependent anion channel(VDAC) proteins are abundant, pore-forming proteins belonging to the eukaryotic mitochondrial porins.　It was discovered in the mitochondrial outer membrane. It also is expressed in the plasma membrane. At least three different VDAC genes have been identified in vertebrates. VDAC proteins are known to play an essential role in cellular metabolism and in the early stages of apoptosis. For example, VDAC contitutes a major pathway by which metabolites such as ADP/ATP, succinate and citrate are exchanged between the cytosol and mitochondria. And VDAC1 in the plasma membrane establishes a novel level of apoptosis regulation putatively via its redox activity.

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Heparin cofactor II (HCII), a single chain glycoprotein with a MW of 65kDa, is a serine protease inhibitor that is synthesized by the liver and circulates in plasma. Heparin cofactor II inhibits thrombin by formation of a stable bimolecular complex, but has no activity against other proteases involved in coagulation or fibrinolysis. The rate at which HCII inhibits thrombin increases more than 1000-fold in the presence of heparin, heparan sulfate, or dermatan sulfate. Heparin cofactor II is unique among serine protease inhibitors in its ability to be stimulated by dermatan sulfate, and it binds to a minor subpopulation of dermatan sulfate oligosaccharides. Turnover studies of labeled HCII in humans suggest that 40% of the protein equilibrates with an extravascular compartment, but the distribution of HCII in various tissues has not been thoroughly investigated. Heparin cofactor II has been detected in the intima of normal human arteries, and the ability of dermatan sulfate in the arterial wall to stimulate HCII is decreased in atherosclerotic lesions.

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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.

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The Rb protein (pRb, 110kDa) is a tumor suppressor, which plays a pivotal role in the negative control of the cell cycle and in tumor progression. pRb is responsible for a major G1 checkpoint, blocking S-phase entry and cell growth. pRb prevents the cell from replicating damaged DNA by preventing its progression through the cell cycle into its S phase or progressing through G1 phase. pRb can actively inhibit cell cycle progression when it is dephosphorylated while this function is inactivated when pRb is phosphorylated. pRb is activated near the end of mitosis (M phase) when a phosphatase dephosphorylates it, allowing it to bind E2F. The pRb protein represses gene transcription, required for transition from G1 to S phase, by directly binding to the transactivation domain of E2F and by binding to the promoter of these genes as a complex with E2F.

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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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Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O₂ byits heme (iron-containing porphyrin) prosthetic group in the center aroundwhich the remaining apoprotein folds. Myoglobin is a single-chain globular protein of 153 amino acids and an early indicator of cardiac ischemia that achieves maximal sensitivity 3 to 4 hours after symptom onset.

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Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes.
Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels.
Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is
regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios.
The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay.

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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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CAD (caspase-activated DNase), a 40kDa nuclear protein, is primarily responsible for cell-autonomous DNA degradation during apoptosis. CAD is present in healthy cells where it is held in an inactive state through the association with its inhibitor ICAD. The ICAD protein is inactivated in apoptotic cells via caspase-3 cleavage thereby releasing CAD, which subsequently cleaves chromosomal DNA. CAD is a magnesium-dependent endonuclease specific for double stranded DNA that generates double strand breaks with 3'-hydroxyl ends. The nuclease preferentially attacks chromatin in the internucleosomal linker DNA. However, the nuclease hypersensitive sites can be detected and CAD is potentially involved in large-scale DNA fragmentation as well. CAD-mediated DNA fragmentation triggers chromatin condensation that is another hallmark of apoptosis.

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ζ-chain associated protein kinase, ZAP70, is a 70 kDa member of the Syk family kinase predominantly involved in T cell receptor (TCR) signaling. It is structurally homologous to Syk, a PTK that is involved in proximal BCR signaling. ZAP-70 is a key signaling molecule in T cell activation and also plays a role in apoptosis and cell migration.
SYK family tyrosine kinases contain a C-terminal kinase domain and tandem N-terminal SH2 domains that bind phosphorylated ITAMs (immunoreceptor tyrosine-based activation motif). Linker region that contains multiple tyrosines separates the SH2 domains from the kinase domain. Phosphorylated tyrosines act as docking sites for phospholipase Cγ1 (PLCγ1).
ZAP-70 and Syk are functionally homologous in antigen receptor signaling. Expression of ZAP-70 in Syk− B cells reconstitutes SCR function. Reconstitution requires the presence of functional Src homology 2 (SH2) and catalytic domains of ZAP-70.
Expression of ZAP-70 is an important negative prognostic factor in chronic lymphocytic leukemia (CLL) with more rapid disease progression and shorter survival.