80 Results for: "Fluorescein diacetate&amp"

Supplier: SIGMA ALDRICH MICROSCOPY

Fluorescein diacetate (FDA) is a non-fluorescent molecule, which is hydrolysed to fluorescent fluorescein in live cells. Dead cells cannot accumulate or hydrolyse FDA. Fluorescein diacetate has been used for the differentiation of live cells from dead cells.

Supplier: Apollo Scientific

Fluorescein diacetate

Supplier: TCI

Fluorescein diacetate ≥98.0% (by HPLC)

Supplier: Thermo Fisher Scientific

Fluorescein diacetate 97%, pure

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

The protein encoded by this gene can hydrolyze substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester, and AMP-NH2. The encoded protein interacts with these substrates via a histidine triad motif, which is part of the loop that binds to the substrate. This gene has been found to be a tumor suppressing gene. Several transcript variants, but only one of them protein-coding, have been found for this gene. [provided by RefSeq, Dec 2012].

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Bioss

Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor.

Supplier: Bioss

Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities.

Supplier: Bioss

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq].

Supplier: Bioss

AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.

Supplier: Bioss

Adenylsuccinate lyase is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. It catalyzes two reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to give aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to give AMP. Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and , in some cases, growth retardation associated with muscle wasting and epilepsy. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

This gene encodes a member of the inositol monophosphatase family. The encoded protein is localized to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). Mutations in this gene are a cause of GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of this gene is located on the long arm of chromosome 1.

Supplier: Bioss

This gene encodes a membrane-bound adenylate cyclase that catalyses the formation of cyclic AMP from ATP and is inhibitable by calcium. The product of this gene is a member of the adenylyl cyclase class-4/guanylyl cyclase enzyme family that is characterized by the presence of twelve membrane-spanning domains in its sequences. [provided by RefSeq, Jul 2008].

Supplier: Bioss

By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function.

Supplier: Bioss

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation.

Supplier: MP Biomedicals

Fluorescein diacetate

Supplier: Merck Millipore (Calbiochem‎)

Fluorescein diacetate, Sigma-Aldrich®

Supplier: Bioss

Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea.

Supplier: Bioss

Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP >IDP >UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

G protein-coupled receptors (GPCRs), also designated seven transmembrane (7TM) receptors and heptahelical receptors, are a protein family which interact with G proteins (heterotrimeric GTPases) to synthesize intracellular second messengers such as diacylglycerol, cyclic AMP, inositol phosphates, and calcium ions. Their diverse biological functions range from vision and olfaction to neuronal and endocrine signaling and are involved in many pathological conditions. G protein receptor 128 (GPR128), a member of the secretin family of GCPRs with a GPS domain in its N-terminal domain, may mediate signaling processes to the interior of the cell via activation of G proteins. GPR128 represents an allopeptide which may be involved in T cell mediated transplant rejection as it is able to stimulate 2.102 T cells.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

L glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. Glutamatergic neurotransmission is involved in most aspects of normal brain function and can be perturbed in many neuropathologic conditions. The metabotropic glutamate receptors are a family of G protein coupled receptors, that have been divided into 3 groups on the basis of sequence homology, putative signal transduction mechanisms, and pharmacologic properties. Group I includes GRM1 and GRM5 and these receptors have been shown to activate phospholipase C. Group II includes GRM2 and GRM3 while Group III includes GRM4, GRM6, GRM7 and GRM8. Group II and III receptors are linked to the inhibition of the cyclic AMP cascade but differ in their agonist selectivities.

Supplier: Bioss

G protein-coupled receptors (GPCRs), also designated seven transmembrane (7TM) receptors and heptahelical receptors, are a protein family which interact with G proteins (heterotrimeric GTPases) to synthesize intracellular second messengers such as diacylglycerol, cyclic AMP, inositol phosphates, and calcium ions. Their diverse biological functions range from vision and olfaction to neuronal and endocrine signaling and are involved in many pathological conditions. G protein receptor 128 (GPR128), a member of the secretin family of GCPRs with a GPS domain in its N-terminal domain, may mediate signaling processes to the interior of the cell via activation of G proteins. GPR128 represents an allopeptide which may be involved in T cell mediated transplant rejection as it is able to stimulate 2.102 T cells.

Supplier: AAT BIOQUEST

FDA is a non-fluorescent hydrophobic fluorescein derivative that can pass through the cell membrane whereupon intracellular esterases hydrolyze the diacetate group producing the highly fluorescent product fluorescein.