You Searched For: 2-Bromo-N-fmoc-L-phenylalanine

Catalog Number: (BTIUBNUM0012-50)

Supplier: Biotium

Description: Recognizes a cluster of proteins between 70-80 kDa, identified as tyrosinase. Occasionally a minor band at 55 kDa is also detected. This MAb shows no cross-reaction with MAGE-1 and tyrosinase-related protein 1, TRP-1/gp75. Tyrosinase is a copper-containing metalloglycoprotein that catalyzes several steps in the melanin pigment biosynthetic pathway; the hydroxylation of tyrosine to L-3,4-dihydroxy-phenylalanine (dopa), and the subsequent oxidation of dopa to dopaquinone. Mutations of the tyrosinase gene occur in various forms of albinism. Tyrosinase is one of the targets for cytotoxic T-cell recognition in melanoma patients. Staining of melanomas with this MAb shows tyrosinase in melanotic as well as amelanotic variants. This MAb is a useful marker for melanocytes and melanomas.

UOM: 1 * 50 µl

Catalog Number: (BOSSBS-13145R-CY3)

Supplier: Bioss

Description: Aminoacyl-tRNA synthetases consist of a family of enzymes that catalyze the specific aminoacylation of tRNA by their cognate amino acid in the initial step of ribosome-dependent protein biosynthesis. FARSLA, also known as FRSA, CML33, FARSL or PheHA (phenylalanyl-tRNA synthetase, alpha subunit), is a member of the class-II aminoacyl-tRNA synthetase family and is highly expressed in proliferating cells of bone marrow. FARSLA is a cytoplasmic phenylalanine-tRNA synthetase that functions as a heterodimer consisting of a catalytic alpha-subunit and a regulatory beta-subunit. The alpha-subunit is responsible for forming the amino acid binding pocket, mediating the ATP/aminoacyl adenylate binding, and interacts with the acceptor stem of the tRNA. FARSLA functions in a cell cycle-dependent and differentiation-dependent manner.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13145R-A647)

Supplier: Bioss

Description: Aminoacyl-tRNA synthetases consist of a family of enzymes that catalyze the specific aminoacylation of tRNA by their cognate amino acid in the initial step of ribosome-dependent protein biosynthesis. FARSLA, also known as FRSA, CML33, FARSL or PheHA (phenylalanyl-tRNA synthetase, alpha subunit), is a member of the class-II aminoacyl-tRNA synthetase family and is highly expressed in proliferating cells of bone marrow. FARSLA is a cytoplasmic phenylalanine-tRNA synthetase that functions as a heterodimer consisting of a catalytic alpha-subunit and a regulatory beta-subunit. The alpha-subunit is responsible for forming the amino acid binding pocket, mediating the ATP/aminoacyl adenylate binding, and interacts with the acceptor stem of the tRNA. FARSLA functions in a cell cycle-dependent and differentiation-dependent manner.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13145R-FITC)

Supplier: Bioss

Description: Aminoacyl-tRNA synthetases consist of a family of enzymes that catalyze the specific aminoacylation of tRNA by their cognate amino acid in the initial step of ribosome-dependent protein biosynthesis. FARSLA, also known as FRSA, CML33, FARSL or PheHA (phenylalanyl-tRNA synthetase, alpha subunit), is a member of the class-II aminoacyl-tRNA synthetase family and is highly expressed in proliferating cells of bone marrow. FARSLA is a cytoplasmic phenylalanine-tRNA synthetase that functions as a heterodimer consisting of a catalytic alpha-subunit and a regulatory beta-subunit. The alpha-subunit is responsible for forming the amino acid binding pocket, mediating the ATP/aminoacyl adenylate binding, and interacts with the acceptor stem of the tRNA. FARSLA functions in a cell cycle-dependent and differentiation-dependent manner.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0121R-CY5.5)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-0121R-A647)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-13145R-A680)

Supplier: Bioss

Description: Aminoacyl-tRNA synthetases consist of a family of enzymes that catalyze the specific aminoacylation of tRNA by their cognate amino acid in the initial step of ribosome-dependent protein biosynthesis. FARSLA, also known as FRSA, CML33, FARSL or PheHA (phenylalanyl-tRNA synthetase, alpha subunit), is a member of the class-II aminoacyl-tRNA synthetase family and is highly expressed in proliferating cells of bone marrow. FARSLA is a cytoplasmic phenylalanine-tRNA synthetase that functions as a heterodimer consisting of a catalytic alpha-subunit and a regulatory beta-subunit. The alpha-subunit is responsible for forming the amino acid binding pocket, mediating the ATP/aminoacyl adenylate binding, and interacts with the acceptor stem of the tRNA. FARSLA functions in a cell cycle-dependent and differentiation-dependent manner.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13442R-CY5)

Supplier: Bioss

Description: GSTZ1 is a member of the glutathione S transferase (GSTs) super family, encoding multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme also plays a significant role in the catabolism of phenylalanine and tyrosine. Several transcript variants of this gene encode multiple protein isoforms. GSTZ1 shows minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. It has low glutathione peroxidase activity with T butyl and cumene hydroperoxides and is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. Highest expression in liver followed by kidney, skeletal muscle and brain. Also expressed in melanocytes, synovium, placenta, breast and fetal liver and heart.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11784R-CY3)

Supplier: Bioss

Description: 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

Supplier: APOLLO SCIENTIFIC

Description: Fmoc-D-Pentafluorophenylalanine

Catalog Number: (APOSOR0491-500G)

Supplier: APOLLO SCIENTIFIC

Description: N-Fmoc-L-leucine

UOM: 1 * 500 g

Catalog Number: (BOSSBS-12941R-FITC)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-13442R-CY7)

Supplier: Bioss

Description: GSTZ1 is a member of the glutathione S transferase (GSTs) super family, encoding multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme also plays a significant role in the catabolism of phenylalanine and tyrosine. Several transcript variants of this gene encode multiple protein isoforms. GSTZ1 shows minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. It has low glutathione peroxidase activity with T butyl and cumene hydroperoxides and is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. Highest expression in liver followed by kidney, skeletal muscle and brain. Also expressed in melanocytes, synovium, placenta, breast and fetal liver and heart.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12942R)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-12942R-A350)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-12941R-A750)

Supplier: Bioss

Description: 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