You Searched For: L(+)-Arginine


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Catalog Number: (BOSSBS-7908R-HRP)
Supplier: Bioss
Description: Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6992R-CY5.5)
Supplier: Bioss
Description: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8499R-A750)
Supplier: Bioss
Description: The function of RED is currently unknown. The protein encoded by the RED gene was identified by its RED repeat, a stretch of repeated arginine, glutamic acid and aspartic acid residues. The protein localises to discrete dots within the nucleus, excluding the nucleolus. This gene maps to chromosome 5; however, a pseudogene may exist on chromosome 2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6992R-A350)
Supplier: Bioss
Description: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6735R-CY5.5)
Supplier: Bioss
Description: SR-A1 (serine arginine-rich pre-mRNA splicing factor) is a member of the SR protein family, which interacts with the C-terminal domain of the large subunit of RNA polymerase II and involved in pre-mRNA splicing. The SR-A1 gene is located on chromosome 19q13.3-q13.4. Overexpression of SR-A1 is found in aggressive ovarian cancers.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6735R-CY3)
Supplier: Bioss
Description: SR-A1 (serine arginine-rich pre-mRNA splicing factor) is a member of the SR protein family, which interacts with the C-terminal domain of the large subunit of RNA polymerase II and involved in pre-mRNA splicing. The SR-A1 gene is located on chromosome 19q13.3-q13.4. Overexpression of SR-A1 is found in aggressive ovarian cancers.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6735R-A555)
Supplier: Bioss
Description: SR-A1 (serine arginine-rich pre-mRNA splicing factor) is a member of the SR protein family, which interacts with the C-terminal domain of the large subunit of RNA polymerase II and involved in pre-mRNA splicing. The SR-A1 gene is located on chromosome 19q13.3-q13.4. Overexpression of SR-A1 is found in aggressive ovarian cancers.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7908R-A750)
Supplier: Bioss
Description: Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12515R-CY5)
Supplier: Bioss
Description: ASL is a member of the lyase 1 family of proteins and is predominantly expressed in the liver. Localizing to the cytoplasm and existing as a homotetramer, ASL catalyzes the hydrolytic cleavage of argininosuccinic acid (ASA) to fumarate and arginine, an essential step of the urea cycle which is crucial for the detoxification of ammonia. This reaction is also involved in the biosynthesis of arginine. In addition, ASL shares high sequence homology with the avian and reptilian eye lens protein, d-crystallin. Mutations in the gene encoding ASL leads to an accumulation of ASA in body fluids and results in Arginosuc-cinic aciduria (ASAuria), an autosomal recessive disorder that is characterized by hyperammonemia, liver enlargement, convulsions, physical and mental retardation, episodic unconsciousness and dry and brittle hair showing trich-orrhexis nodosa (weak points or nodes in the hair shaft).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12515R-A555)
Supplier: Bioss
Description: ASL is a member of the lyase 1 family of proteins and is predominantly expressed in the liver. Localizing to the cytoplasm and existing as a homotetramer, ASL catalyzes the hydrolytic cleavage of argininosuccinic acid (ASA) to fumarate and arginine, an essential step of the urea cycle which is crucial for the detoxification of ammonia. This reaction is also involved in the biosynthesis of arginine. In addition, ASL shares high sequence homology with the avian and reptilian eye lens protein, d-crystallin. Mutations in the gene encoding ASL leads to an accumulation of ASA in body fluids and results in Arginosuc-cinic aciduria (ASAuria), an autosomal recessive disorder that is characterized by hyperammonemia, liver enlargement, convulsions, physical and mental retardation, episodic unconsciousness and dry and brittle hair showing trich-orrhexis nodosa (weak points or nodes in the hair shaft).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6992R-A680)
Supplier: Bioss
Description: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) <i>in vitro</i>. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localisation to the meiotic nuage. Methylates RPS10.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6992R-A750)
Supplier: Bioss
Description: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) <i>in vitro</i>. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localisation to the meiotic nuage. Methylates RPS10.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10501R-CY3)
Supplier: Bioss
Description: This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10255R-CY7)
Supplier: Bioss
Description: The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8499R-A350)
Supplier: Bioss
Description: The function of RED is currently unknown. The protein encoded by the RED gene was identified by its RED repeat, a stretch of repeated arginine, glutamic acid and aspartic acid residues. The protein localizes to discrete dots within the nucleus, excluding the nucleolus. This gene maps to chromosome 5; however, a pseudogene may exist on chromosome 2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6735R)
Supplier: Bioss
Description: SR-A1 (serine arginine-rich pre-mRNA splicing factor) is a member of the SR protein family, which interacts with the C-terminal domain of the large subunit of RNA polymerase II and involved in pre-mRNA splicing. The SR-A1 gene is located on chromosome 19q13.3-q13.4. Overexpression of SR-A1 is found in aggressive ovarian cancers.
UOM: 1 * 100 µl


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