35929 Results for: "2-Amino-4-methylbenzoic acid"

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It is well known that the control of gene expression involves activation of protein kinase cascades that regulate transcription factors within the nucleus (Karin and Hunter, 1995). The cyclic AMP response element binding protein (CREB) is one of the best characterized stimulus-induced transcription factors (Montminy, 1997). This transcription factor is a component of intracellular signaling events that regulate a wide range of biological functions, from spermatogenesis to circadian rhythms and memory (Shaywitz and Greenberg, 1999; Silva et al., 1998). A variety of protein kinases including protein kinase A (PKA), mitogenactivated protein kinases (MAPKs), and Ca2+/calmodulin-dependent protein kinases (CaMKs) phosphorylate CREB at serine 133 (Ser133), and phosphorylation of Ser133 are required for CREB-mediated transcription (Johannessen et al., 2004; Kornhauser et al., 2002).

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Tryptophan hydroxylase (TPH) catalyzes the 5-hydroxylation of tryptophan, which is the first step in the biosynthesis of indoleamines (serotonin and melatonin) (Martinez et al., 2001). In mammals, serotonin biosynthesis occurs predominantly in neurons which originate in the Raphe nuclei of the brain, and melatonin synthesis takes place within the pineal gland. Although TPH catalyzes the same reaction within the Raphe nuclei and the pineal gland, TPH activity is rate-limiting for serotonin but not melatonin biosynthesis. Serotonin functions mainly as a neurotransmitter, whereas melatonin is the principal hormone secreted by the pineal gland. The activity of TPH is enhanced by phosphorylation by cAMP-dependent protein kinase (PKA) and Ca2+/calmodulin kinase II (CaM K II) (Jiang et al., 2000; Johansen et al., 1996). CaM K II phosphorylates Ser19 which lies within the regulatory domain of TPH2 (McKinney et

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Mouse monoclonal IgG2b antibody against human, rhesus, cynomolgus CD20, PerCP-Cy5.5-conjugated.

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The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR). The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death. The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits.

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EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vanderhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cell-to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work demonstrated that Tyr331 of EphrinB was phosphorylated in HEK293 cells after stimulation by the soluble EphB2 receptor tyrosine kinase (Kalo et al., 2001).

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Human monoclonal IgG1 antibody against SARS-CoV-2 (2019-nCoV) S protein (HEK293-expressed recombinant).

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The original QuikChange Site-Directed Mutagenesis Kits speed up and simplify site-directed mutagenesis studies. The kits eliminate the need for sub-cloning into M13-based bacteriophage vectors and for ss-DNA rescue. This allows oligo-mediated introduction of site-specific mutations into virtually any double-stranded plasmid DNA. In addition, the XL version of the kit is specially designed for efficient mutagenesis of large (4 to 14 kb) or otherwise difficult-to mutagenise plasmid templates. The XL kit features components specifically designed for more efficient DNA replication and bacterial transformation.

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BDNF belongs to the neurotrophin family and regulates the survival and differentiation of neurons during development. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. FUNCTION: Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. POst translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family.

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Mouse monoclonal IgG2b antibody against human, rhesus, cynomolgus CD20, PE-conjugated.

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EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vanderhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cell-to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work suggests that phosphorylation of a specific EphrinB residue (Tyr298) plays a key role in EphrinB signaling (Kalo, et al., 2001).

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The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). Phosphorylation of Tyr1336 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002) and ischemia may also increase the phosphorylation of this site (Takagi et al., 2003).

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The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). It has been shown that phosphorylation of Ser1480 disrupts the interaction of NR2B with the PDZ domains of PSD-95 and SAP102 and decreases surface NR2B expression in neurons (Chung et al., 2004).

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The supplement kit for endothelial cell proliferation medium is suitable for culturing Provitro human endothelial cells after adding the supplement kit components to 500 ml basal medium The formulation is optimised for initial seeding of 4000 cells/cm² up to confluence (approx. 90%). Feeder-layer, matrix substrates or other substances are not necessary. Due to the possibility of reduced proliferative activity we recommend to use the antibiotic supplement for freshly isolated cells only. The supplement kit for endothelial cell priliferation medium is thoroughly tested after each production. All components are tested in a stringent biological assay. Each batch is checked for human endothelial cells proliferating characteristics. The cells cultured in endothelial cell growth medium are checked regarding their morphology, the adherence rate, the colony forming efficiency and the population doubling time.

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Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14. PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels. MMP2 isoform 2 mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways. Catalytic activity of MMP2 causes cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. (Ref: uniprot.org).

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Mouse monoclonal IgG2b antibody against human, rhesus, cynomolgus CD20, Alexa Fluor® 488-conjugated.

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Chimeric mouse (V), human (C) monoclonal IgG antibody against SARS-CoV, SARS-CoV-2 (2019-nCoV) S protein (HEK293-expressed recombinant).

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EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vancerhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cellto cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work suggests that phosphorylation of a specific EphrinB residue (Tyr298) plays a key role in EphrinB signaling (Kalo, et al., 2001).

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14-3-3 proteins are a family of highly conserved proteins that appear to have multiple roles in cell signaling (Bridges and Moorhead, 2005). The proteins are abundantly expressed in the brain and have been detected in the cerebrospinal fluid of patients with different neurological disorders (Berg et al., 2003). 14-3-3 proteins bind protein ligands that are typically phosphorylated on
serine or threonine residues and regulate the functions of these binding partners by a number of different mechanisms (Silhan et al., 2004; Dougherty and Morrison, 2004). The14-3-3 proteins affect a diverse array of cellular processes including the cell cycle and transcription, signal transduction and intracellular trafficking. These functions of 14-3-3 proteins are facilitated by, if not dependent on, its dimeric structure. Recent work has demonstrated that the dimeric status of the 14-3-3 protein is regulated by site-specific serine phosphorylation (Woodcock et al., 2003).

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GDNF is a glycosylated, disulfide-bonded homodimer molecule. It was first discovered as a potent survival factor for midbrain dopaminergic neurons and was then shown to rescue these neurons in animal models of Parkinson's disease. GDNF is about 100 times more efficient survival factor for spinal motor neurons than the neurotrophins. FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Secreted protein. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. DISEASE: Defects in GDNF may be a cause of Hirschsprung disease (HSCR). In association with mutations of RET gene, defects in GDNF may be involved in Hirschsprung disease. This genetic disorder of neural crest development is characterized by the absence of intramural ganglion cells in the hindgut, often resulting in intestinal obstruction. DISEASE: Defects in GDNF are a cause of congenital central hypoventilation syndrome (CCHS); also known as congenital failure of autonomic control or Ondine curse. CCHS is a rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.