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Procurou por: Adaptadores+Múltiplos


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Descrição: Cell cycle progression is controlled in part by a family of cyclin proteins and cyclin dependent kinases (Cdks). Cdk proteins work in concert with the cyclins to phosphorylate key substrates involved in each phase of cell cycle progression. Specifically, Cdk2 interacts with Cyclins A, B1, B3, D, or E to control cell cycle progression. The Cyclin-dependent kinase 2-interacting protein (CINP) interacts with components of the replication complex and Cdk2 and Cdc7, thereby providing a functional and physical link between Cdk2 and Cdc7 during firing of the origins of replication. However, CINP is phopshorylated by Cdc7, but not by Cdk2. CINP also interacts with ATR-interacting protein and regulates ATR-dependent signaling, resistance to replication stress and G2 checkpoint integrity.
Código de Artigo: BOSSBS-9077R-A488
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Cell cycle progression is controlled in part by a family of cyclin proteins and cyclin dependent kinases (Cdks). Cdk proteins work in concert with the cyclins to phosphorylate key substrates involved in each phase of cell cycle progression. Specifically, Cdk2 interacts with Cyclins A, B1, B3, D, or E to control cell cycle progression. The Cyclin-dependent kinase 2-interacting protein (CINP) interacts with components of the replication complex and Cdk2 and Cdc7, thereby providing a functional and physical link between Cdk2 and Cdc7 during firing of the origins of replication. However, CINP is phopshorylated by Cdc7, but not by Cdk2. CINP also interacts with ATR-interacting protein and regulates ATR-dependent signaling, resistance to replication stress and G2 checkpoint integrity.
Código de Artigo: BOSSBS-9077R-HRP
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: The membranes of myelinating Schwann cells are joined by tight, gap and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-Lanterman and mesaxons. Tight junctions help establish polarity in mammalian epithelia by forming a physical barrier that separates apical and basolateral membranes. Pals-associated tight junction protein (PATJ), the human homolog of Drosophila Discs Lost, is differentially localized in myelinating Schwann cells. PATJ associates with Claudin-1, CRB1 (a transmembrane protein that plays a role in epithelial cell polarity and photoreceptor development), and Pals1 (a Lin-7 associated protein). The PATJ/Pals1/CRB1 complex can form a tripartite tight junction in epithelial cells crucial to their integrity.
Código de Artigo: BOSSBS-12142R-HRP
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: The PSD-95/SAP 90 family of proteins, which are known to bind to and cluster various membrane proteins, are involved in the organization of synaptic structure. These proteins are physically and functionally linked to cytoskeletal and/or signaling proteins. CRIPT (for cysteine-rich interactor of PDZ three), a novel postsynaptic protein, binds specifically to the PDZ3 domain of PSD-95/SAP 90. CRIPT induces the recruitment of PSD-95/SAP 90 to microtubules, and it has been shown to bind directly to microtubules, indicating that it may be responsible for cytoskeletal anchoring of PSD-95/SAP 90. CRIPT is widely expressed outside of the brain and is highly conserved from animals to plants suggesting a wider role in regulating cytoskeleton-membrane associations.
Código de Artigo: BOSSBS-11021R-A647
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: The PSD-95/SAP 90 family of proteins, which are known to bind to and cluster various membrane proteins, are involved in the organization of synaptic structure. These proteins are physically and functionally linked to cytoskeletal and/or signaling proteins. CRIPT (for cysteine-rich interactor of PDZ three), a novel postsynaptic protein, binds specifically to the PDZ3 domain of PSD-95/SAP 90. CRIPT induces the recruitment of PSD-95/SAP 90 to microtubules, and it has been shown to bind directly to microtubules, indicating that it may be responsible for cytoskeletal anchoring of PSD-95/SAP 90. CRIPT is widely expressed outside of the brain and is highly conserved from animals to plants suggesting a wider role in regulating cytoskeleton-membrane associations.
Código de Artigo: BOSSBS-11021R-FITC
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Dorfin is a multi-pass membrane, RING-IBR type, E3 ubiquitin-protein ligase. It is widely expressed with highest levels found in heart and ubiquitous expression throughout the central nervous system. Dorfin functions by accepting ubiquitin in the form of a thioester from UBCH7 and UBC8 and then transferring it to the targeted substrates. Dorfin is responsible for ubiquitylating synphilin-1, CaSR and mutant variants of SOD-1, a protein at fault for familial ALS (amyotrophic lateral sclerosis). Dorfin physically interacts with VCP (Valosin-containing protein) via its C-terminus. Together these two proteins are associated with the formation of ubiquitylated inclusions (UBIs) that characterize many neurodegenerative disorders, such as Parkinson's disease and ALS. This association with UBIs suggests that Dorfin plays an important role in the disease process.
Código de Artigo: BOSSBS-11778R-A750
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Dorfin is a multi-pass membrane, RING-IBR type, E3 ubiquitin-protein ligase. It is widely expressed with highest levels found in heart and ubiquitous expression throughout the central nervous system. Dorfin functions by accepting ubiquitin in the form of a thioester from UBCH7 and UBC8 and then transferring it to the targeted substrates. Dorfin is responsible for ubiquitylating synphilin-1, CaSR and mutant variants of SOD-1, a protein at fault for familial ALS (amyotrophic lateral sclerosis). Dorfin physically interacts with VCP (Valosin-containing protein) via its C-terminus. Together these two proteins are associated with the formation of ubiquitylated inclusions (UBIs) that characterize many neurodegenerative disorders, such as Parkinson’s disease and ALS. This association with UBIs suggests that Dorfin plays an important role in the disease process.
Código de Artigo: BOSSBS-11778R-A488
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Predominantly localized to the nucleolus, BOP1 (Block of proliferation 1 protein) is a 746 amino acid highly conserved non-ribosomal protein that is involved in ribosome biogenesis. Truncation of the amino terminus of BOP1 leads to cell growth arrest in the G1 phase and specific inhibition of 28S and 5.8S rRNA synthesis, as well as a deficit in the cytosolic 60S ribosomal subunit. This suggests that BOP1 is involved in the formation of mature rRNAs and in the biogenesis of the 60S ribosomal subunit. BOP1 physically interacts with pescadillo (a protein involved in cell proliferation) and enables efficient incorporation of pescadillo into the nucleolar preribosomal complexes, thereby affecting rRNA maturation and the cell cycle. The BOP1-pescadillo complex is also necessary for biogenesis of 60S ribosomal subunits. Deregulation of BOP1 may lead to colorectal tumorigenesis.
Código de Artigo: BOSSBS-12877R-CY5
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Encoding over 300 genes, chromosome 18 contains about 76 million bases. Trisomy 18, or Edwards syndrome, is the second most common trisomy after Downs syndrome. Symptoms of Edwards syndrome include low birth weight, a variety of physical development defects, heart deformations and breathing difficulty. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are associated with chromosome 18. The TGF_ modulators, Smad2, Smad4 and Smad7 are encoded by chromosome 18. The C18orf56 gene product has been provisionally designated C18orf56 pending further characterisation.
Código de Artigo: BOSSBS-9675R-A750
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: CCDC11 is a 514 amino acid protein encode by a gene that maps to human chromosome 18q21.1. Encoding over 300 genes, chromosome 18 contains about 76 million bases. Trisomy 18, or Edwards syndrome, is the second most common trisomy after Downs syndrome. Symptoms of Edwards syndrome include low birth weight, a variety of physical development defects, heart deformations and breathing difficulty. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are associated with chromosome 18. The TGF∫ modulators, Smad2, Smad4 and Smad7 are encoded by chromosome 18.
Código de Artigo: BOSSBS-7740R-FITC
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: The membranes of myelinating Schwann cells are joined by tight, gap and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-Lanterman and mesaxons. Tight junctions help establish polarity in mammalian epithelia by forming a physical barrier that separates apical and basolateral membranes. Pals-associated tight junction protein (PATJ), the human homolog of Drosophila Discs Lost, is differentially localized in myelinating Schwann cells. PATJ associates with Claudin-1, CRB1 (a transmembrane protein that plays a role in epithelial cell polarity and photoreceptor development), and Pals1 (a Lin-7 associated protein). The PATJ/Pals1/CRB1 complex can form a tripartite tight junction in epithelial cells crucial to their integrity.
Código de Artigo: BOSSBS-12142R-CY7
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Cell cycle progression is controlled in part by a family of cyclin proteins and cyclin dependent kinases (Cdks). Cdk proteins work in concert with the cyclins to phosphorylate key substrates involved in each phase of cell cycle progression. Specifically, Cdk2 interacts with Cyclins A, B1, B3, D, or E to control cell cycle progression. The Cyclin-dependent kinase 2-interacting protein (CINP) interacts with components of the replication complex and Cdk2 and Cdc7, thereby providing a functional and physical link between Cdk2 and Cdc7 during firing of the origins of replication. However, CINP is phopshorylated by Cdc7, but not by Cdk2. CINP also interacts with ATR-interacting protein and regulates ATR-dependent signaling, resistance to replication stress and G2 checkpoint integrity.
Código de Artigo: BOSSBS-9077R-CY3
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.
Código de Artigo: BOSSBS-5798R-CY5
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: The PSD-95/SAP 90 family of proteins, which are known to bind to and cluster various membrane proteins, are involved in the organization of synaptic structure. These proteins are physically and functionally linked to cytoskeletal and/or signaling proteins. CRIPT (for cysteine-rich interactor of PDZ three), a novel postsynaptic protein, binds specifically to the PDZ3 domain of PSD-95/SAP 90. CRIPT induces the recruitment of PSD-95/SAP 90 to microtubules, and it has been shown to bind directly to microtubules, indicating that it may be responsible for cytoskeletal anchoring of PSD-95/SAP 90. CRIPT is widely expressed outside of the brain and is highly conserved from animals to plants suggesting a wider role in regulating cytoskeleton-membrane associations.
Código de Artigo: BOSSBS-11021R-CY3
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Cell cycle progression is controlled in part by a family of cyclin proteins and cyclin dependent kinases (Cdks). Cdk proteins work in concert with the cyclins to phosphorylate key substrates involved in each phase of cell cycle progression. Specifically, Cdk2 interacts with Cyclins A, B1, B3, D, or E to control cell cycle progression. The Cyclin-dependent kinase 2-interacting protein (CINP) interacts with components of the replication complex and Cdk2 and Cdc7, thereby providing a functional and physical link between Cdk2 and Cdc7 during firing of the origins of replication. However, CINP is phopshorylated by Cdc7, but not by Cdk2. CINP also interacts with ATR-interacting protein and regulates ATR-dependent signaling, resistance to replication stress and G2 checkpoint integrity.
Código de Artigo: BOSSBS-9077R-A750
UOM: 1 * 100 µl
Fornecedor: Bioss


Descrição: Cell cycle progression is controlled in part by a family of cyclin proteins and cyclin dependent kinases (Cdks). Cdk proteins work in concert with the cyclins to phosphorylate key substrates involved in each phase of cell cycle progression. Specifically, Cdk2 interacts with Cyclins A, B1, B3, D, or E to control cell cycle progression. The Cyclin-dependent kinase 2-interacting protein (CINP) interacts with components of the replication complex and Cdk2 and Cdc7, thereby providing a functional and physical link between Cdk2 and Cdc7 during firing of the origins of replication. However, CINP is phopshorylated by Cdc7, but not by Cdk2. CINP also interacts with ATR-interacting protein and regulates ATR-dependent signaling, resistance to replication stress and G2 checkpoint integrity.
Código de Artigo: BOSSBS-9077R-A350
UOM: 1 * 100 µl
Fornecedor: Bioss


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