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Key Documents

MAB318-AF488

Sigma-Aldrich

Anti-Tyrosine Hydroxylase Antibody, clone LNC1, Alexa Fluor 488 Conjugate

clone LNC1, from mouse, ALEXA FLUOR 488

Sinónimos:

Tyrosine 3-monooxygenase, Tyrosine Hydroxylase, Tyrosine 3-hydroxylase, TH

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

ALEXA FLUOR 488

antibody form

purified antibody

antibody product type

primary antibodies

clone

LNC1, monoclonal

species reactivity

human, chicken, mouse, frog, zebrafish, rat

technique(s)

immunocytochemistry: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... TH(7054)
rat ... Th(25085)

General description

Tyrosine 3-monooxygenase (EC 1.14.16.2; UniProt P07101; also known as Dystonia 14, TH, Tyrosine 3-hydroxylase) is encoded by the TH (also known as DYT14, DYT5b, TYH) gene (Gene ID 7054) in human. Tyrosine hydroxylase plays an important role in the physiology of adrenergic neurons. It is the first and rate-limiting enzyme involved in the biosynthesis of the catecholamines Dopamine and Norepinephrine from tyrosine. TH is, therefore, a useful marker for dopaminergic and noradrenergic neurons. TH enzymatic activity requires ferrous ions as cofactors and is believed to be regulated by phosphorylation. Six isoforms of human TH exist as a result of alternative splicing (UniProt P07101-1 through P07101-6).

Specificity

Recognizes an epitope on the outside of the regulatory N-terminus of tyrosine hydroxylase. Does not react with dopamine-beta-hydroxylase, phenylalanine hydroxylase, trytophan hydroxylase, dehydropteridine reductase, sepiapterin reductase, or phenethanolamine-N-methyl transferase (PNMT) by Western blotting using the unconjugated antibody (Cat. No. MAB318).

Immunogen

Epitope: On the outside of the regulatory N-terminus of tyrosine hydroxylase.
Tyrosine Hydroxylase purified from PC12 cells.

Application

Anti-Tyrosine Hydroxylase Antibody, clone LNC1, Alexa Fluor 488 Conjugate is an antibody against Tyrosine Hydroxylase for use in Immunocytochemistry.
Research Category
Neuroscience
Research Sub Category
Developmental Neuroscience
The unconjugated antibody (Cat. No. MAB318) is shown to be suitable also for Western blotting, immunohistochemistry, and immunoprecipitation applications.

Quality

Evaluated by Immunocytochemistry in rat cortical neurons.

Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected Tyrosine Hydroxylase in rat cortical neurons.

Target description

~59-63 kDa observed

Physical form

Protein A purified
Purified mouse antibody conjugate in PBS with 15 mg/mL BSA and 0.1 % sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Legal Information

ALEXA FLUOR is a trademark of Life Technologies

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.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Kara A Fulton et al.
eLife, 10 (2021-05-14)
A dense reconstruction of neuronal synaptic connectivity typically requires high-resolution 3D electron microscopy (EM) data, but EM data alone lacks functional information about neurons and synapses. One approach to augment structural EM datasets is with the fluorescent immunohistochemical (IHC) localization
Dasiel O Borroto-Escuela et al.
Neurochemical research, 45(1), 5-15 (2019-06-07)
G protein-coupled receptors modulate the synaptic glutamate and GABA transmission of the claustrum. The work focused on the transmitter-receptor relationships in the claustral catecholamine system and receptor-receptor interactions between kappa opioid receptors (KOR) and SomatostatinR2 (SSTR2) in claustrum. Methods used

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