Anti-Tyrosine Hydroxylase Antibody, clone 2/40/15 ZooMAb^® Mouse Monoclonal

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ZooMAb antibodies represent an entirely new generation of recombinant monoclonal antibodies.

Each ZooMAb antibody is manufactured using our proprietary recombinant expression system, purified to homogeneity, and precisely dispensed to produce robust and highly reproducible lot-to-lot consistency. Only top-performing clones are released for use by researchers. Each antibody is validated for high specificity and affinity across multiple applications, including its most commonly used application. ZooMAb antibodies are reliably available and ready to ship when you need them.

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Clone 2/40/15 is a ZooMAb mouse recombinant monoclonal antibody that specifically detects Tyrosine-3 Hydroxylase.

Purified tyrosine hydroxylase from a rat pheochromocytoma.

Anti-Tyrosine Hydroxylase, clone 2/40/15 ZooMAb, Cat. No. ZMS1033, is a recombinant Mouse monoclonal antibody that detects Tyrosine Hydroxylase and is tested for use in Immunocytochemistry, Immunohistochemistry (Paraffin), and Western Blotting.

Immunohistochemistry (Paraffin) Analysis: A 1:100 dilution from a representative lot detected Tyrosine Hydroxylase in rat brain and human brain tissue sections.

Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected Tyrosine Hydroxylase in PC12 cells.

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user

Tyrosine 3-monooxygenase (UniProt: P04177; also known as EC: 1.14.62.2, Tyrosine 3-hydroxylase, TH) is encoded by the Th gene (Gene ID: 25085) in rat. Tyrosine hydroxylase acts as a rate-limiting enzyme of catecholamine biosynthesis. It hydroxylates tyrosine to L-DOPA and then L- DOPA is converted to dopamine by aromatic amino acid decarboxylase. Tyrosine hydroxylase requires tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Its activity is regulated by phosphorylation at four different serine residues by multiple protein kinases. The N-terminal region of tyrosine hydroxylase plays a critical role in controlling its catalytic activity. Its catalytic domain is located in the C-terminal region and binds the substrates and the cofactor. Its activity is inhibited by a feedback mechanism by catecholamines. Dopamine is shown to bind to tyrosine hydroxylase competitively with tetrahydrobiopterin and interacts with the regulatory domain. Tyrosine hydroxylase activity can be modified in the presence of nitric oxide that results in nitration of tyrosine residues. Tyrosine hydroxylase deficiency leads to impaired synthesis of dopamine as well as epinephrine and norepinephrine and significantly reduced tyrosine hydroxylase activity and dopamine levels are reported in the brain of Parkinson s disease subjects. This ZooMAb recombinant monoclonal antibody, generated by our propriety technology, offers significantly enhanced specificity, affinity, reproducibility, and stability over conventional monoclonals. (Ref.: Daubner SC et al., (2011). Arch. Biochem. Biophys. 508(1): 1-12).

Purified recombinant mouse monoclonal antibody IgG, lyophilized in PBS, 5% Trehalose, normal appearance a coarse or translucent resin. Contains no biocide or preservatives, such as azide, or any animal by-products. Larger pack sizes provided as multiples of 25 μL.

Recommend storage of lyophilized product at 2-8°C; Before reconstitution, micro-centrifuge vials briefly to spin down material to bottom of the vial; Reconstitute each vial by adding 25 μL of filtered lab grade water or PBS; Reconstituted antibodies can be stored at 2-8°C, or -20°C for long term storage. Avoid repeated freeze-thaws.

ZooMAb is a registered trademark of Merck KGaA, Darmstadt, Germany

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.