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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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Anti-NF2 Mouse Monoclonal Antibody [clone: AF1G4]

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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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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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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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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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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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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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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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Recombinant protein used to causes an allergic reaction in human.

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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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RAF is the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway. The mammalian Raf family of serine/threonine kinases consists of three highly conserved members: A-Raf, B-Raf, and Raf-1 (or c-Raf-1). Each isoform has three conserved regions in common: CR1, CR2, and CR3. Raf isoforms vary in their cell-specific expression and potency of kinase activity. Cytosolic C-Raf ubiquitously expressed in adult tissues, with highest expression in muscle, cerebellum, and fetal brain. Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites. Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301 and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events.

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Son of sevenless (SOS) is a guanine nucleotide exchange factor that
activates Ras in response to growth factor stimulation. Sos1, and its
closely related Sos2 paralog, are comprised of an N-terminal
histone-binding domain, a RacGEF catalytic (DH) domain juxtaposed with
a PH domain, a Ras exchanger motif (REM) domain, a RasGEF catalytic
domain, and a C-terminal proline-rich region. Sos1 catalyzes the
GDP-GTP exchange within the membrane-bound GTPase Ras and
thereby switches on a key signaling circuit that involves the activation of
MAPK cascade central to cellular proliferation, survival and differentiation.
Growth factor stimulation rapidly induces the phosphorylation of Sos on
multiple serine and threonine sites. Phosphorylation of residues within the
Sos C-terminus by the MAP/ERK kinase disrupts the Grb2-Sos complex.

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In vivo, tyrosine phosphorylation is reversible and dynamic; the phosphorylation states are governed by the opposing activites of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). PTPs are involved in controlling of diverse array of cellular process. They are large(~100) and structurally diverse family of enzymes. PTPs contain one or two catalytic domains which is approximately 280 residues and are characterized by the existence of the signature motif HC(X)5R. The Cys and Arg residues in this motif have essential functions for catalytic activity. PTPs regulate cell growth and metabolism, with special emphasis on its ability to regulate integrin, growth factor, and cytokine signaling.

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Akt (protein kinase B, PKB) is a serine/threonine protein kinase. Akt is activated by PI3 kinase, which is itself activated by tyrosine kinase (Thr308, Ser473). Akt/PKB controls vital cellular functions such as cell survival/apoptosis, cell cycle progression and glucose metabolism. It also acts down-stream from growth factors and hormones. Akt/PKB can inhibit cell cycle arrest by phosphorylating p21. Also, Akt/PKB may potentiate cell cycle progression through increased translation of cyclin D. Akt/PKB directly affects the apoptosis pathway by, for example, targeting the pro-apoptotic Bcl-2 related protein, BAD. It also can phosphorylate three kinases upstream of SAPK. The SAPK system consists of two groups of kinases, and JNK and p38 MAP kinase pathways. The SAPK pathway is an important target for Akt/PKB regulation to promote cell survival. Akt/PKB is able to regulate cell survival through transcriptional factors(Forkhead, nuclear factor-kB(NF-kB), Murine double minute 2(Mdm2)) that are responsible for pro- as well as anti-apoptotic genes. One of the first physiological targets of PKB to be identified was glycogen synthase kinase-3(GSK3), which has been associated with the control of many cellular processes, including glycogen and protein synthesis, and the modulation of transcription factor activity. The involvement of Akt in disease processes like malignancy, neurodegeneration and abnormal glucose metabolism has also been demonstrated.

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Casein kinases are a group of ubiquitous Ser/Thr kinases that phosphorylate key regulatory proteins involved in the control of cell differentiation, proliferation, chromosome segregation, circadian rhythms, and metabolic pathways. CK1 family members share a highly conserved kinase domain but differ in their variable N- and C-terminal domains.
Mammals have seven family members: α, β, γ1, γ2, γ3, δ and epsilon. They all share at least 50% amino
acid identity within the protein kinase catalytic domain. CK1 isoforms exclusively use ATP as phosphate donor and are generally co-factor independent.
Casein kinase I epsilon is a Wnt-regulated kinase, and regulated phosphorylation of Dvl allows fine tuning of the Wnt-b-catenin signaling pathway. CKIe positively regulates Akt possibly by inhibiting PP2A. CKIe
play an important role in neurodegenerative diseases.

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Well known as detoxification enzymes, the glutathione transferases(GST) also function in prostaglandin and steroid hormone synthesis. The enzymes are dimmers of 25kDa subunits. There are three major groups of GSTs: canonical(or cytosolic) GSTs(cGSTs), mitochondrial GSTs, and microsomal GSTs. GSTs play a role in the metabolism of drugs, pesticides and other xenobiotics.
GST is also a widely used fusion partner, since it offers both an easily detectable tag and a simple purification process that has a minimal with little effect on the biological function of the protein of interest. Recombinant hybrids containing a polypeptide fusion partner (termed “affinity tag”) to facilitate the purification of the target polypeptides are widely used. Epitope tags are useful for the labeling and detection of proteins using immunoblotting, IP and immunostaining techniques. Due to their small size, they are unlikely to affect the tagged protein’s biochemical properities. Numerous vectors containing GST-tags have been developed for both prokaryotic and eukaryotic systems over the past decade.

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