Choose Your Country or Region

Tyrosine Hydroxylase (L1F21) Rabbit mAb

Catalog No.: F3538

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IHC1:150 - 1:600 IF1:50 - 1:200 FCM1:400 - 1:1600

Application
WB, IHC, IF, FCM

Reactivity
Human, Mouse, Rat

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
55-60 kDa

Datasheet & SDS

Biological Description

Specificity
Tyrosine Hydroxylase (L1F21) Rabbit mAb recognizes endogenous levels of total tyrosine hydroxylase protein.

Clone
L1F21

Synonym(s)
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase (TH), TH, TYH

Background
Tyrosine hydroxylase (TyrH) is the rate-limiting enzyme in catecholamine biosynthesis, catalyzing the conversion of tyrosine to DOPA using tetrahydrobiopterin and molecular oxygen. Its N-terminal 150 amino acids form a regulatory domain that controls enzyme activity through multiple mechanisms. Regulation occurs via phosphorylation at four serine residues by various kinases and dephosphorylation by two phosphatases. Serine sites within the regulatory domain include Ser9, Ser31, and Ser40. Phosphorylation at Ser40 by protein kinase A (PKA) boosts catalytic function, while phosphorylation at Ser31 by cyclin-dependent kinase 5 (CDK5) enhances activity by stabilizing the protein. TyrH is subject to feedback inhibition by catecholamine neurotransmitters such as dopamine that compete with tetrahydrobiopterin for binding and interact with the regulatory domain. Activity is also influenced by protein–protein interactions with enzymes in the catecholamine and tetrahydrobiopterin pathways, chaperone-like structural proteins modulating neuronal redox state, and the vesicular transporter responsible for dopamine storage. Post-translational modifications include nitration of tyrosine and glutathionylation of cysteine residues in response to nitric oxide.

Background

Tyrosine hydroxylase (TyrH) is the rate-limiting enzyme in catecholamine biosynthesis, catalyzing the conversion of tyrosine to DOPA using tetrahydrobiopterin and molecular oxygen. Its N-terminal 150 amino acids form a regulatory domain that controls enzyme activity through multiple mechanisms. Regulation occurs via phosphorylation at four serine residues by various kinases and dephosphorylation by two phosphatases. Serine sites within the regulatory domain include Ser9, Ser31, and Ser40. Phosphorylation at Ser40 by protein kinase A (PKA) boosts catalytic function, while phosphorylation at Ser31 by cyclin-dependent kinase 5 (CDK5) enhances activity by stabilizing the protein. TyrH is subject to feedback inhibition by catecholamine neurotransmitters such as dopamine that compete with tetrahydrobiopterin for binding and interact with the regulatory domain. Activity is also influenced by protein–protein interactions with enzymes in the catecholamine and tetrahydrobiopterin pathways, chaperone-like structural proteins modulating neuronal redox state, and the vesicular transporter responsible for dopamine storage. Post-translational modifications include nitration of tyrosine and glutathionylation of cysteine residues in response to nitric oxide.

References
https://pubmed.ncbi.nlm.nih.gov/21176768/ https://pubmed.ncbi.nlm.nih.gov/15471880/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
If you have any other enquiries, please leave a message.

* Indicates a Required Field

Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%