You Searched For: L(+)-Arginine

Catalog Number: (BOSSBS-6659R-FITC)

Supplier: Bioss

Description: 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.

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Supplier: ENZO LIFE SCIENCES

Description: The non-protein amino acid L-canavanine is an analog of L-arginine. Selective inducible nitric oxide synthase (iNOS; NOS II) inhibitor. Induces apoptotic cell death and shows antiproliferative and immunotoxic effects.

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Catalog Number: (BOSSBS-1930R-A555)

Supplier: Bioss

Description: Vasopressin, also known as arginine vasopressin (AVP) or antidiuretic hormone (ADH), is a posterior pituitary hormone that is synthesised in the hypothalamus. Vasopressin is synthesised as a precursor protein that consists of arginine vasopressin and two associated proteins, neurophysin 2 and the glycopeptide copeptin. Vasopressin, together with its carrier protein neurophysin II, is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis, where it is either stored or secreted into the bloodstream. Vasopressin acts as a growth factor by enhancing pH regulation through acid-base transport systems. It has a direct antidiuretic action on the kidney and also causes vasoconstriction of the peripheral vessels. Vasopressin can also contract smooth muscle during parturition and lactation. It also plays a role in cognition, tolerance, adaptation and complex sexual and maternal behaviour, as well as in the regulation of water excretion and cardiovascular functions. Mutations in the vasopressin precursor cause autosomal dominant neurohypophyseal diabetes insipidus (ADNDI), which is characterised by persistant thirst, polydipsia and polyuria.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1930R-A647)

Supplier: Bioss

Description: Vasopressin, also known as arginine vasopressin (AVP) or antidiuretic hormone (ADH), is a posterior pituitary hormone that is synthesised in the hypothalamus. Vasopressin is synthesised as a precursor protein that consists of arginine vasopressin and two associated proteins, neurophysin 2 and the glycopeptide copeptin. Vasopressin, together with its carrier protein neurophysin II, is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis, where it is either stored or secreted into the bloodstream. Vasopressin acts as a growth factor by enhancing pH regulation through acid-base transport systems. It has a direct antidiuretic action on the kidney and also causes vasoconstriction of the peripheral vessels. Vasopressin can also contract smooth muscle during parturition and lactation. It also plays a role in cognition, tolerance, adaptation and complex sexual and maternal behaviour, as well as in the regulation of water excretion and cardiovascular functions. Mutations in the vasopressin precursor cause autosomal dominant neurohypophyseal diabetes insipidus (ADNDI), which is characterised by persistant thirst, polydipsia and polyuria.

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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.

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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.

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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.

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Catalog Number: (BOSSBS-10501R)

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].

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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.

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Catalog Number: (BOSSBS-6735R-A680)

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.

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Catalog Number: (BOSSBS-6735R-A350)

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.

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Catalog Number: (BOSSBS-10255R)

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.

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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

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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

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Catalog Number: (BOSSBS-1930R)

Supplier: Bioss

Description: Vasopressin, also known as arginine vasopressin (AVP) or antidiuretic hormone (ADH), is a posterior pituitary hormone that is synthesised in the hypothalamus. Vasopressin is synthesised as a precursor protein that consists of arginine vasopressin and two associated proteins, neurophysin 2 and the glycopeptide copeptin. Vasopressin, together with its carrier protein neurophysin II, is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis, where it is either stored or secreted into the bloodstream. Vasopressin acts as a growth factor by enhancing pH regulation through acid-base transport systems. It has a direct antidiuretic action on the kidney and also causes vasoconstriction of the peripheral vessels. Vasopressin can also contract smooth muscle during parturition and lactation. It also plays a role in cognition, tolerance, adaptation and complex sexual and maternal behaviour, as well as in the regulation of water excretion and cardiovascular functions. Mutations in the vasopressin precursor cause autosomal dominant neurohypophyseal diabetes insipidus (ADNDI), which is characterised by persistant thirst, polydipsia and polyuria.

UOM: 1 * 100 µl

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Supplier: G-Biosciences

Description: Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues and typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. The distribution of these residues in proteins allows trypsin digestion to produce peptides that are readily identified by mass spectrometry.