943 Résultats pour : "AbFrontier"

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Anti-Peroxiredoxin 6 Rabbit Polyclonal Antibody

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Anti-Alpha/ Beta-Synuclein Rabbit Polyclonal Antibody

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Anti-IRAK4 Rabbit Polyclonal Antibody

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Bone morphogenetic protein 4, also known as BMP4, is a member of the bone morphogenetic protein family which is part of the transforming growth factor-β superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo. BMPs also regulate cell proliferation, differentiation, lineage determination, motility, and death.
BMP4 is a potent bone-inducing morphogen, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.
BMP4 is a critical signaling molecule required for the early differentiation of the embryo and establishing of a dorsal-ventral axis. It also plays a role in the epithelial-mesenchymal interactions leading to tooth formation.
Both BMP2 and BMP4 have been found in calcified atherosclerotic plaques and aortic valve diseases, which suggests their importance in cardiovascular diseases.

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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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Check point kinase 1 (Chk1) is a serine / threonine protein kinase and a key mediator in the DNA damage-induced checkpoint network. Chk1 is an evolutionarily conserved protein kinase that functions to ensure genomic integrity upon genotoxic stress. When the G2 or S checkpoint is abrogated
by the inhibition of Chk1, p53-deficient cancer cells undergo mitotic catastrophe and eventually apoptosis, whereas normal cells are still arrested in the G1 phase. Thus, Chk1 inhibitors can preferentially
potentiate the efficacy of DNA damaging agents in cancer cells, and Chk1 is an attractive therapeutic target for cancer treatment, especially since approximately 50% of all human cancers are p53-deficient.

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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 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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Lactate dehydrogenase (LDH) is the enzyme in the glycolytic pathway that converts pyruvate to lactate with concomitant interconversion of NADH and NAD+. In mammals, the enzyme is encoded by three genes: LDHA (M or muscle form), LDHB (H or heart form), and LDHC (X or testis form). The three human LDHs have 84–89% sequence similarities and 69–75% amino acid identities. There are five different LDH isoenzymes based on the proportion of M and H chains existing in the LDH tetrameric structure.
The LDHA is hypoxia inducible and its expression is directly controlled by the transcriptional activity of the hypoxia inducible factor 1a (HIF1a). LDHB is also known to be upregulated in many cancers.

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Lactate dehydrogenase (LDH) is the enzyme in the glycolytic pathway that converts pyruvate to lactate with concomitant interconversion of NADH and NAD+. In mammals, the enzyme is encoded by three genes: LDHA (M or muscle form), LDHB (H or heart form), and LDHC (X or testis form). The three human LDHs have 84–89% sequence similarities and 69–75% amino acid identities. There are five different LDH isoenzymes based on the proportion of M and H chains existing in the LDH tetrameric structure.
The LDHA is hypoxia inducible and its expression is directly controlled by the transcriptional activity of the hypoxia inducible factor 1a (HIF1a). LDHB is also known to be upregulated in many cancers.

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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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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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Recombinant protein used to causes an allergic reaction in human.

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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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Histone H2A is one of the 5 main histone proteins involved in the structure of chromatin in eukaryotic cells. The nucleosome in which an 147 base-pairs of DNA are wrapped 1.7 times around a central core of eight histone protein molecules forms the basic building block of chromatin. Histone octamer consists of two copies each of H2A, H2B, H3, and H4 histones.
Histone H2A variant H2AX, a component of the nucleosome core structure that comprises 10%–15% of total cellular H2A, has a special role in DNA repair, cell cycle checkpoints, regulated gene recombination events, and tumor suppression.
H2AX can be phosphorylated on Ser 1, acetylated on Lys 5 and ubiquitinated on Lys 119. But what makes H2AX unique is a highly conserved serine 139 residue which is rapidly phosphorylated upon the exposure of cells to DNA damage. H2AX is phosphorylated by ATR in response to DNA replication stress, and primarily by ATM in response to low levels of ionizing radiation. Phosphorylation of H2AX increases the likelihood of assembling a functional repair complex by increasing the local concentration of repair factors near the lesion.

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The inhibitor of caspase-3-activated DNase (ICAD) is a caspase-3 substrate that controls nuclear apoptosis. ICAD has two isoforms: a functional isoform of M.W. 45kDa, ICAD-L/DNA fragmentation factor (DFF) 45; and a M.W.35kDa isoform, ICAD-S/DFF35. Although both ICAD-L and ICAD-S can bind and inhibit CAD, only ICAD-L was reported to be functional. ICAD is cleaved to be inactivated and allow caspase-activated DNase (CAD) to execute nuclear internucleosomal apoptotic DNA fragmentation. In non-apoptotic cells, CAD is complexed with its inhibitor, ICAD. The activation of the CAD/ICAD complex occurs through the caspase 3-mediated cleavage of ICAD at residues 117 and 224, which results in three ICAD fragments that are then released from CAD. In addition to its DNase inhibitory activity, ICAD acts as a CAD-specific folding chaperone. There are recent reports that ICAD is a potential target for restoring a normal apoptotic signal transduction pathway in colon and brain cancer cells.

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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 cystein 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).

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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. ROCK1 is involved in diverse cellular functions, including smooth muscle contraction, actin cytoskeleton organization, cell adhesion and motility, and gene expression.

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Serum amyloid P component (SAP) is a normal plasma protein and a universal non-fibrillar constituent of amyloid deposits. SAP is a member of the pentraxin protein family which includes C-reactive protein. Human SAP is secreted and catabolized only by hepatocytes, and consists of five identical non-covalently associated subunits, each with a molecular mass of 25 kDa, which are non-covalently associated in a pentameric disc-like ring. SAP is a calcium-dependent ligand binding protein, which binds to DNA and chromatin, and to all known types of amyloid fibrils accounting for its specific accumulation in amyloid deposits. Serum amyloid P component scintigraphy is a non-invasive and quantitative method for imaging amyloid deposits, which produces diagnostic images in most patients with systemic amyloidosis, and can be used repeatedly to monitor the course of the disease.

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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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Transthyretin (TTR, 55 kDa homotetramer) is a thyroid hormone-binding protein that transports thyroxine (T4) from the bloodstream to the brain. TTR was originally called prealbumin because it ran faster than albumin on electrophoresis gels. . TTR is produced in the liver and circulates in the bloodstream, where it binds retinol and thyroxine. TTR is suggested that plays an essential role in brain function. The protein consists of around 130 amino acids, which assemble as a homotetramer that contains an internal channel in which T4 is bound. Within this complex, T4 appears to be transported across the blood-brain barrier, where, in the choroid plexus, the hormone stimulates further synthesis of transthyretin. The protein then diffuses back into the bloodstream, where it binds T4 for transport back to the brain. TTR is known to be associated with the amyloid diseases senile systemic amyloidosis (SSA), familial amyloid polyneuropathy (FAP), and familial amyloid cardiomyopathy (FAC).

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SHP2 is a tyrosine phosphatase containing two tandem SH2 (src homology 2) domains. Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Together with tyrosine kinases, PTPs regulate the phosphorylation state of many important signaling molecules.
SHP1 and SHP2 represent a subfamily of non-transmembrane PTPs that contain two SH2 domains followed by a PTP domain. Tyrosine phosphorylation of SHP2 is required for normal ERK activation in response to some growth factors. In the inactive state, the N-terminal SH2 domain binds the PTP domain and blocks access of potential substrates to the active site. This auto-inhibition is relieved by the binding of phosphopeptides to SH2 domain, resulting in activation of phostphatase activity.
Noonan syndrome characterized by an abnormal face, short stature and cardiac abnormalities is due to the mutations of N-terminal SH2 domain or PTP domain. SHP2 mutations might also cause some leukemia, and could be important in pathogenesis by Helicobacter pylori, the major cause of gastric ulcer and carcinoma.

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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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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 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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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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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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Protein phosphatase-1(PP1) is one of the major Ser/Thr protein phosphatases and is ubiquitous in eukaryotic cells. PP1 is localized to its site of action by interacting with targeting or regulatory proteins, a majority of which contains a primary docking site referred to as the RVXF/W motif. The catalytic subunit of PP1 exists as three isoforms, PP1a, PP1b, and PP1r. The PP1 catalytic subunits are small proteins of 37kDa, which are highly conserved, with their main differences falling in the C-term. The PP1 catalytic subunit exists in the cell in complex with a large number of targeting/regulatory subunits, thereby generating different enzyme forms that allow it to perform a diverse number of cellular functions.

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Moesin (for membrane-organizing extension spike protein) is a member of the EMR protein family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons.

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Human carboxypeptidase N (CPN) [(EC) 3.4.17.3], a member of the CPN/E subfamily of “regulatory” metallo-carboxypeptidases, is a zinc metalloprotease, which cleaves basic amino acids, lysine and arginine, from the carboxy-terminus of biologically active peptides and proteins.
CPN is an extracellular glycoprotein synthesized in the liver and secreted into the blood, where it controls the activity of vasoactive peptide hormones, growth factors and cytokines by specifically removing C-terminal basic residues. Human CPN was discovered as an enzyme that inactivates bradykinin by cleaving its carboxy-terminal arginine and was also referred to as kininase I.
CPN is a major inactivator of anaphylatoxins C3a, C4a and C5a and also cleaves off C-terminal Lys residues from larger protein substrates, such as the M and B subunits of creatine kinase, released from the heart after myocardial infarction.
CPN is a tetramer (280 kDa) comprised of two heterodimers each
consisting of a catalytic CPN1(48 – 55 kDa) and non-catalytic CPN2 (83kDa) subunit.The CPN2 subunit keeps the smaller catalytic subunit in the circulation and protects it against inactivation at 37 °C. The CPN2 subunit may also promote the cleavage of higher molecular mass plasma protein substrates by the catalytic CPN1 subunit.
The most conserved region of the carboxypeptidase proteins is the active site. All mammalian carboxypeptidases contain a zinc binding site, a substrate binding site, an amino acid involved in peptide specificity, and an amino acid involved in catalytic activity of the protein.
Patients with reduced CPN level present chronic recurrent angioedema, which is unrelated to diet or environment.