You Searched For: Boc-2-nitro-L-phenylalanine

Supplier: MP Biomedicals

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

Catalog Number: (BOSSBS-15472R-CY5)

Supplier: Bioss

Description: HGD is a 445 amino acid protein that belongs to the homogentisate dioxygenase family and is involved in the pathway of amino acid degradation. Expressed at high levels in kidney, colon, liver, prostate and small intestine, HGD uses iron as a cofactor to catalyse the oxygen-dependent conversion of homogentisate to 4-maleylacetoacetate, a reaction that is the fourth step in the creation of L-phenylalanine from fumarate and acetoacetic acid. Defects in the gene encoding HGD are the cause of alkaptonuria (AKU), an autosomal recessive disorder that is characterised by urine that turns dark on standing and alkalinisation, black ochronotic pigmentation of cartilage and collagenous tissues and spine arthritis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-15472R-A647)

Supplier: Bioss

Description: HGD is a 445 amino acid protein that belongs to the homogentisate dioxygenase family and is involved in the pathway of amino acid degradation. Expressed at high levels in kidney, colon, liver, prostate and small intestine, HGD uses iron as a cofactor to catalyse the oxygen-dependent conversion of homogentisate to 4-maleylacetoacetate, a reaction that is the fourth step in the creation of L-phenylalanine from fumarate and acetoacetic acid. Defects in the gene encoding HGD are the cause of alkaptonuria (AKU), an autosomal recessive disorder that is characterised by urine that turns dark on standing and alkalinisation, black ochronotic pigmentation of cartilage and collagenous tissues and spine arthritis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-15472R-A488)

Supplier: Bioss

Description: HGD is a 445 amino acid protein that belongs to the homogentisate dioxygenase family and is involved in the pathway of amino acid degradation. Expressed at high levels in kidney, colon, liver, prostate and small intestine, HGD uses iron as a cofactor to catalyse the oxygen-dependent conversion of homogentisate to 4-maleylacetoacetate, a reaction that is the fourth step in the creation of L-phenylalanine from fumarate and acetoacetic acid. Defects in the gene encoding HGD are the cause of alkaptonuria (AKU), an autosomal recessive disorder that is characterised by urine that turns dark on standing and alkalinisation, black ochronotic pigmentation of cartilage and collagenous tissues and spine arthritis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12933R-CY7)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12933R)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Supplier: SIGMA ALDRICH MICROSCOPY

Description: NLO material.

Catalog Number: (BOSSBS-12933R-A680)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyse other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesised in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Catalog Number: (85897.180)

Supplier: VWR Chemicals

Description: nitro-Molybdovanadic Reag. Ph. Eur. 1060100

UOM: 1 * 200 mL

Certificates

Catalog Number: (BOSSBS-12933R-A488)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12933R-A647)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12933R-A350)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12933R-A555)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

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.

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.

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.