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Numero del catalogo: (BOSSBS-0121R-A488)
Proveedor: Bioss
Descripción: SYAP1 (synapse-associated protein 1) is a 352 amino acid protein that is ubiquitously expressed in adult tissues. SYAP1 contains one BSD domain which is a novel domain that is present in basal transcription factors, synapse-associated proteins and several hypothetical proteins. The BSD domain is characterized by three predicted alpha helices and by conserved tryptophan and phenylalanine residues, located at the C-terminus of the domain. The gene that encodes SYAP1 in humans is located on chromosome X. Chromosome X consists of about 153 million base pairs and nearly 1,000 genes. Color blindness, hemophilia, and Duchenne muscular dystrophy are well known X chromosome-linked conditions which affect males more frequently as males carry a single X chromosome.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12941R-A680)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterised by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5 to 10 fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12941R-HRP)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12942R-A680)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterised by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5 to 10 fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-11784R-A647)
Proveedor: Bioss
Descripción: SPR, also known as sepiapterin reductase, is a homodimeric cytoplasmic protein that belongs to the sepiapterin reductase family. SPR functions as an NADH-dependent aldo-keto reductase and specifically catalyzes the reduction of pteridine derivatives. In addition, SPR plays an important role in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the final reduction step of the synthesis pathway. BH4 is an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine) and is required for proper dopamine synthesis. Mutations in the gene encoding SPR can cause sepiapterin reductase deficiency, a monoamine neurotransmitter deficiency without hyperphenylalaninemia. Sepiapterin reductase deficiency interferes with BH4 synthesis, resulting in DOPA-responsive dystonia and a variety of other human diseases. In addition, SPR mRNA expression is increased in the brain of Parkinson’s Disease (PD) patients, suggesting that SPR may play a role in PD.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-11784R-A750)
Proveedor: Bioss
Descripción: SPR, also known as sepiapterin reductase, is a homodimeric cytoplasmic protein that belongs to the sepiapterin reductase family. SPR functions as an NADH-dependent aldo-keto reductase and specifically catalyses the reduction of pteridine derivatives. In addition, SPR plays an important role in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the final reduction step of the synthesis pathway. BH4 is an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine) and is required for proper dopamine synthesis. Mutations in the gene encoding SPR can cause sepiapterin reductase deficiency, a monoamine neurotransmitter deficiency without hyperphenylalaninemia. Sepiapterin reductase deficiency interferes with BH4 synthesis, resulting in DOPA-responsive dystonia and a variety of other human diseases. In addition, SPR mRNA expression is increased in the brain of Parkinson's Disease (PD) patients, suggesting that SPR may play a role in PD.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-6659R-CY7)
Proveedor: Bioss
Descripción: Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier.
UOM: 1 * 100 µl


Proveedor: MP Biomedicals
Descripción: Soluble in water (30 mg/ml). Also soluble in 1 M HCl (50 mg/ml - clear to slightly hazy solution).

Numero del catalogo: (BOSSBS-12942R-A750)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterised by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5 to 10 fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12942R-A350)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12941R-FITC)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterized by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5- to 10-fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12941R-A750)
Proveedor: Bioss
Descripción: All members of the Src gene family of tyrosine kinases are characterised by a carboxy terminal domain tyrosine which is highly phosphorylated in the inactive form of the enzyme and phosphorylated to a much lesser extent when the enzyme is active. In the case of Src p60, Y527 is this tyrosine; however, a mutant form of c-Src in which Y527 is replaced by phenylalanine is transforming and displays 5 to 10 fold elevated kinase activity compared to its normal counterpart. Csk has been identified as a Src-related tyrosine kinase having both SH2 and SH3 domains and a catalytic domain but lacking sequences amino terminal to the SH3 domain as well as carboxy terminal regulatory sequences. Csk phosphorylates Src on Y527 and also downregulates Lyn, Fyn and Lck by tyrosine phosphorylation of carboxy terminal regulatory sites.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-11784R-A555)
Proveedor: Bioss
Descripción: SPR, also known as sepiapterin reductase, is a homodimeric cytoplasmic protein that belongs to the sepiapterin reductase family. SPR functions as an NADH-dependent aldo-keto reductase and specifically catalyzes the reduction of pteridine derivatives. In addition, SPR plays an important role in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the final reduction step of the synthesis pathway. BH4 is an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine) and is required for proper dopamine synthesis. Mutations in the gene encoding SPR can cause sepiapterin reductase deficiency, a monoamine neurotransmitter deficiency without hyperphenylalaninemia. Sepiapterin reductase deficiency interferes with BH4 synthesis, resulting in DOPA-responsive dystonia and a variety of other human diseases. In addition, SPR mRNA expression is increased in the brain of Parkinson’s Disease (PD) patients, suggesting that SPR may play a role in PD.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-11784R)
Proveedor: Bioss
Descripción: SPR, also known as sepiapterin reductase, is a homodimeric cytoplasmic protein that belongs to the sepiapterin reductase family. SPR functions as an NADH-dependent aldo-keto reductase and specifically catalyzes the reduction of pteridine derivatives. In addition, SPR plays an important role in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the final reduction step of the synthesis pathway. BH4 is an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine) and is required for proper dopamine synthesis. Mutations in the gene encoding SPR can cause sepiapterin reductase deficiency, a monoamine neurotransmitter deficiency without hyperphenylalaninemia. Sepiapterin reductase deficiency interferes with BH4 synthesis, resulting in DOPA-responsive dystonia and a variety of other human diseases. In addition, SPR mRNA expression is increased in the brain of Parkinson’s Disease (PD) patients, suggesting that SPR may play a role in PD.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-11784R-CY5)
Proveedor: Bioss
Descripción: SPR, also known as sepiapterin reductase, is a homodimeric cytoplasmic protein that belongs to the sepiapterin reductase family. SPR functions as an NADH-dependent aldo-keto reductase and specifically catalyzes the reduction of pteridine derivatives. In addition, SPR plays an important role in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the final reduction step of the synthesis pathway. BH4 is an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine) and is required for proper dopamine synthesis. Mutations in the gene encoding SPR can cause sepiapterin reductase deficiency, a monoamine neurotransmitter deficiency without hyperphenylalaninemia. Sepiapterin reductase deficiency interferes with BH4 synthesis, resulting in DOPA-responsive dystonia and a variety of other human diseases. In addition, SPR mRNA expression is increased in the brain of Parkinson’s Disease (PD) patients, suggesting that SPR may play a role in PD.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-6659R-A647)
Proveedor: Bioss
Descripción: Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier.
UOM: 1 * 100 µl


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El stock para este material es limitada pero puede estar disponible en un almacén cerca de usted. Por favor, asegúrese de que ha iniciado sesión en la web para que el stock disponible se puede mostrar. Si el call sigue apareciendo y usted necesita ayuda, por favor llámenos al 902 222 897 o por email en webshop.es@avantorsciences.com.
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Este producto se trata de un artículo regulado sometido a normativa que restringe su venta.
Si procede, nos pondremos en contacto con usted para solicitarle la licencia o declaración de uso necesaria para poder proceder al suministro del producto.
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