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Katalogové číslo: (PRSI29-722)
Dodavatel: ProSci Inc.
Popis: Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD (+) as the electron acceptor and the other NADP (+). Five isocitrate dehydrogenases have been reported: three NAD (+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP (+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD (+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. IDH3A is the alpha subunit of one isozyme of NAD (+)-dependent isocitrate dehydrogenase.Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD (+) as the electron acceptor and the other NADP (+). Five isocitrate dehydrogenases have been reported: three NAD (+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP (+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD (+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the alpha subunit of one isozyme of NAD (+)-dependent isocitrate dehydrogenase.
Měrná jednotka: 1 * 100 µG


Katalogové číslo: (BOSSBS-11238R-A647)
Dodavatel: Bioss
Popis: SH3 and multiple ankyrin repeat domains 1-3 (Shank1-3) of the Shank/ProSAP family are molecular scaffolds in the postsynaptic density (PSD). The PSD is an electron-dense structure underneath the postsynaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the presynaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). Shank recruits betaPIX and PAK to spines to regulate postsynaptic structure and interacts with NMDA receptor and metabotropic glutamate receptor complexes. Transcript splice variation in the Shank family influences the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain to ensure normal development.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11238R-A680)
Dodavatel: Bioss
Popis: SH3 and multiple ankyrin repeat domains 1-3 (Shank1-3) of the Shank/ProSAP family are molecular scaffolds in the postsynaptic density (PSD). The PSD is an electron-dense structure underneath the postsynaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the presynaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localisation of ion channels, receptors, Signalling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). Shank recruits betaPIX and PAK to spines to regulate postsynaptic structure and interacts with NMDA receptor and metabotropic glutamate receptor complexes. Transcript splice variation in the Shank family influences the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain to ensure normal development.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11238R-CY7)
Dodavatel: Bioss
Popis: SH3 and multiple ankyrin repeat domains 1-3 (Shank1-3) of the Shank/ProSAP family are molecular scaffolds in the postsynaptic density (PSD). The PSD is an electron-dense structure underneath the postsynaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the presynaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). Shank recruits betaPIX and PAK to spines to regulate postsynaptic structure and interacts with NMDA receptor and metabotropic glutamate receptor complexes. Transcript splice variation in the Shank family influences the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain to ensure normal development.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11198R-CY7)
Dodavatel: Bioss
Popis: The ProSAP family of proteins contain many protein-protein interaction domains and serve as scaffolding mediators within the post-synaptic density (PSD) of excitatory brain synapses. The PSD is an electron-dense structure underneath the post-synaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the pre-synaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). ProSAPiP1 (proline rich synapse associated protein interacting protein 1) is a 673 amino acid protein that interacts with the PDZ domain of Shank 3. ProSAPiP1 expression is brain-specific with highest expression within the cerebellum, hippocampus and cerebral cortex.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-15538R)
Dodavatel: Bioss
Popis: Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the beta subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Jul 2008].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (PRSI26-297)
Dodavatel: ProSci Inc.
Popis: Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD (+) as the electron acceptor and the other NADP (+). Five isocitrate dehydrogenases have been reported: three NAD (+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP (+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP (+)-dependent isozyme is a homodimer. IDH2 is the NADP (+)-dependent isocitrate dehydrogenase found in the mitochondria. It plays a role in intermediary metabolism and energy production. This protein may tightly associate or interact with the pyruvate dehydrogenase complex.Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD (+) as the electron acceptor and the other NADP (+). Five isocitrate dehydrogenases have been reported: three NAD (+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP (+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP (+)-dependent isozyme is a homodimer. The protein encoded by this gene is the NADP (+)-dependent isocitrate dehydrogenase found in the mitochondria. It plays a role in intermediary metabolism and energy production. This protein may tightly associate or interact with the pyruvate dehydrogenase complex. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
Měrná jednotka: 1 * 50 µG


Katalogové číslo: (BOSSBS-11198R)
Dodavatel: Bioss
Popis: The ProSAP family of proteins contain many protein-protein interaction domains and serve as scaffolding mediators within the post-synaptic density (PSD) of excitatory brain synapses. The PSD is an electron-dense structure underneath the post-synaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the pre-synaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). ProSAPiP1 (proline rich synapse associated protein interacting protein 1) is a 673 amino acid protein that interacts with the PDZ domain of Shank 3. ProSAPiP1 expression is brain-specific with highest expression within the cerebellum, hippocampus and cerebral cortex.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (SIAL925977-25G)
Dodavatel: Merck
Popis: Mo2Ti₂AlC₃ is a 413 MAX phase, a precursor for cutting-edge applications. MXene nanosheets, a class of two-dimensional transition-metal carbides, are predicted to serve as high-performing anodes for non-lithium-ion batteries by combined first-principles simulations and experimental measurements. Further, Mo₂Ti₂AlC₃, a novel MAX phase, exhibits impressive thermoelectric properties, surpassing traditional ceramics. Its metallic transport behavior offers new possibilities in electronic applications. Additionally, Mo₂Ti₂AlC₃ serves as an efficient mode-locker for ultrafast fiber lasers, highlighting its versatility in photonics.
Měrná jednotka: 1 * 25 g

New Product


Dodavatel: Biotium
Popis: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.

Dodavatel: Biotium
Popis: Cytochrome C is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of cytochrome c and to induce cell death. The release of cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.

Katalogové číslo: (PRSI5819)
Dodavatel: ProSci Inc.
Popis: IDH1 Antibody: Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Two NADP(+)-dependent isocitrate dehydrogenases have been found as homodimer: IDH1 is predominantly cytosolic and peroxisomal and IDH2 is mitochondrial. The presence of IDH1 in peroxisomes suggests it may play a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic IDH1 serves a significant role in cytoplasmic NADPH production. Defects in IDH1 are involved in the development of glioma.
Měrná jednotka: 1 * 100 µG


Katalogové číslo: (BOSSBS-11238R-CY5)
Dodavatel: Bioss
Popis: SH3 and multiple ankyrin repeat domains 1-3 (Shank1-3) of the Shank/ProSAP family are molecular scaffolds in the postsynaptic density (PSD). The PSD is an electron-dense structure underneath the postsynaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the presynaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). Shank recruits betaPIX and PAK to spines to regulate postsynaptic structure and interacts with NMDA receptor and metabotropic glutamate receptor complexes. Transcript splice variation in the Shank family influences the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain to ensure normal development.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11238R-HRP)
Dodavatel: Bioss
Popis: SH3 and multiple ankyrin repeat domains 1-3 (Shank1-3) of the Shank/ProSAP family are molecular scaffolds in the postsynaptic density (PSD). The PSD is an electron-dense structure underneath the postsynaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the presynaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). Shank recruits betaPIX and PAK to spines to regulate postsynaptic structure and interacts with NMDA receptor and metabotropic glutamate receptor complexes. Transcript splice variation in the Shank family influences the spectrum of Shank-interacting proteins in the PSDs of adult and developing brain to ensure normal development.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11198R-CY5)
Dodavatel: Bioss
Popis: The ProSAP family of proteins contain many protein-protein interaction domains and serve as scaffolding mediators within the post-synaptic density (PSD) of excitatory brain synapses. The PSD is an electron-dense structure underneath the post-synaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the pre-synaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). ProSAPiP1 (proline rich synapse associated protein interacting protein 1) is a 673 amino acid protein that interacts with the PDZ domain of Shank 3. ProSAPiP1 expression is brain-specific with highest expression within the cerebellum, hippocampus and cerebral cortex.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11198R-A555)
Dodavatel: Bioss
Popis: The ProSAP family of proteins contain many protein-protein interaction domains and serve as scaffolding mediators within the post-synaptic density (PSD) of excitatory brain synapses. The PSD is an electron-dense structure underneath the post-synaptic plasma membrane of excitatory synapses that anchors and clusters glutamate receptors opposite to the pre-synaptic neurotransmitter release site. Shank proteins contain PDZ modular domains that coordinate the synaptic localization of ion channels, receptors, signaling enzymes, and cell adhesion molecules. The PDZ domain mediates protein-protein interactions via the recognition of a conserved sequence motif at the C-terminus of their target protein(s). ProSAPiP1 (proline rich synapse associated protein interacting protein 1) is a 673 amino acid protein that interacts with the PDZ domain of Shank 3. ProSAPiP1 expression is brain-specific with highest expression within the cerebellum, hippocampus and cerebral cortex.
Měrná jednotka: 1 * 100 µl


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