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bs-0016P is one synthetic peptide derived from human TH. The protein encoded by this gene is involved in the conversion of tyrosine to dopamine. It is the rate-limiting enzyme in the synthesis of catecholamines, hence plays a key role in the physiology of adrenergic neurons. Mutations in this gene have been associated with autosomal recessive Segawa syndrome. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Jul 2008]

bs-0016P is one synthetic peptide derived from human TH. The protein encoded by this gene is involved in the conversion of tyrosine to dopamine. It is the rate-limiting enzyme in the synthesis of catecholamines, hence plays a key role in the physiology of adrenergic neurons. Mutations in this gene have been associated with autosomal recessive Segawa syndrome. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Jul 2008]

bs-0016P is one synthetic peptide derived from human TH. The protein encoded by this gene is involved in the conversion of tyrosine to dopamine. It is the rate-limiting enzyme in the synthesis of catecholamines, hence plays a key role in the physiology of adrenergic neurons. Mutations in this gene have been associated with autosomal recessive Segawa syndrome. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Jul 2008]

bs-0016P is one synthetic peptide derived from human TH. The protein encoded by this gene is involved in the conversion of tyrosine to dopamine. It is the rate-limiting enzyme in the synthesis of catecholamines, hence plays a key role in the physiology of adrenergic neurons. Mutations in this gene have been associated with autosomal recessive Segawa syndrome. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene. [provided by RefSeq, Jul 2008]

Metallothioneins (MTs) are a family of low molecular weight, heavy metal-binding proteins characterized by a high cysteine content and lack of aromatic amino acids. MTs bind 7 to 12 heavy metal atoms per molecule of protein. They are ubiquitous in the animal and plant kingdoms and are also found in prokaryotes. In mammals, the cysteine residues are absolutely conserved and serve to coordinate heavy metal atoms such as zinc, cadmium, and copper via mercaptide linkages.

Metallothioneins (MTs) are a family of low molecular weight, heavy metal-binding proteins characterized by a high cysteine content and lack of aromatic amino acids. MTs bind 7 to 12 heavy metal atoms per molecule of protein. They are ubiquitous in the animal and plant kingdoms and are also found in prokaryotes. In mammals, the cysteine residues are absolutely conserved and serve to coordinate heavy metal atoms such as zinc, cadmium, and copper via mercaptide linkages.