TH Mouse

Tyrosine Hydroxylase Mouse Recombinant
Cat. No.
BT29432
Source
Sf9, Baculovirus cells.
Synonyms
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). 
TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tyrosine 3-monooxygenase (Th) is the rate-limiting enzyme in catecholamine synthesis. Th uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Th is involved in regulating dopamine (DA) neurotransmission through biosynthesis and reuptake. It plays a critical role in the physiology of adrenergic neurons. Additionally, Th influences the differentiation and function of T helper cells when overexpressed in lymphocytes.
Description
Recombinant Mouse TH, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) with a molecular mass of 57.0 kDa. (Molecular size on SDS-PAGE appears at approximately 50-70 kDa). TH is expressed with a 6 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile, colorless solution.
Formulation
TH protein solution (0.25 mg/mL) in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Greater than 90% purity as determined by SDS-PAGE.
Synonyms
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.

Product Science Overview

Introduction

Tyrosine Hydroxylase (TH), also known as tyrosine 3-monooxygenase, is a critical enzyme in the biosynthesis of catecholamines, which include dopamine, noradrenaline, and adrenaline . This enzyme catalyzes the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in catecholamine synthesis . The recombinant form of Tyrosine Hydroxylase from mouse is often used in research to study its biochemical properties and regulatory mechanisms.

Biochemical Properties

Tyrosine Hydroxylase is a tetrameric enzyme with a theoretical molecular weight of approximately 60 kDa . It requires tetrahydrobiopterin (BH4), molecular oxygen, and ferrous iron (Fe2+) as cofactors for its enzymatic activity . The enzyme’s activity is regulated by various factors, including phosphorylation by protein kinases and feedback inhibition by catecholamines .

Physiological Importance

The physiological importance of Tyrosine Hydroxylase is underscored by its role in the central nervous system and adrenal medulla, where it is involved in the synthesis of neurotransmitters and hormones . Dysregulation of TH activity is associated with several neurological disorders, including Parkinson’s disease, schizophrenia, and dystonia . Studies have shown that targeted disruption of the TH gene in mice results in mid-gestational lethality, highlighting its critical role in development .

Recombinant Mouse Tyrosine Hydroxylase

Recombinant Mouse Tyrosine Hydroxylase is produced using baculovirus expression systems and is often tagged with a His-tag for purification purposes . This recombinant protein is used in various biochemical assays to study the enzyme’s properties, regulatory mechanisms, and interactions with other molecules .

Applications in Research

Recombinant Mouse Tyrosine Hydroxylase is widely used in research to investigate the molecular mechanisms underlying catecholamine biosynthesis and its regulation. It is also used to study the effects of mutations and post-translational modifications on enzyme activity . Additionally, this recombinant protein serves as a valuable tool in drug discovery and development, particularly for conditions related to catecholamine dysregulation .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.