Anti-Tyrosine Hydroxylase Antibody, clone 3M12, ZooMAb® Rabbit Monoclonal

Description

• General description: We are committed to bringing you greener alternative products, which adhere to one or more of The 12 Principles of Green Chemistry.This antibody is Preservative-free, produced without the harm or sacrifice of animals and exceptionally stable to allow for ambient shipping and storage if needed and thus aligns with "Waste Prevention", "Designing Safer Chemicals" and "Design for Energy Efficiency". Click here for more information.
• Specificity: Clone 3M12 is a ZooMAb rabbit recombinant monoclonal antibody that specifically detects Tyrosine Hydroxylase. It targets an epitope with in 15 amino acids from the N-terminal region.
• Immunogen: KLH-conjugated linear peptide corresponding to 15 amino acids from the N-terminal region of rat Tyrosine 3-hydroxylase.
• Application: Anti-Tyrosine Hydroxylase, clone 3M12 ZooMAb, Cat. No. ZRB2381, is a recombinant Rabbit Monoclonal Antibody that specifically targets Tyrosine 3-hydroxylase and has been tested for use in Immunocytochemistry, Immunfluorescence, Immunohistochemistry (Paraffin), and Western Blotting.
• Target description: 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 activity and dopamine levels are shown to be significantly lower in the brain of Parkinson s disease subjects. Tyrosine hydroxylase deficiency leads to impaired synthesis of dopamine as well as epinephrine and norepinephrine. 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).
• Physical form: Purified recombinant rabbit monoclonal antibody IgG, lyophilized in PBS with 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.
• Reconstitution: 30 μg/mL after reconstitution at 25 μL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.
• Storage and Stability: 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.
• Legal Information: ZooMAb is a registered trademark of Merck KGaA, Darmstadt, Germany
• Disclaimer: 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.