T1299
Monoclonal Anti-Tyrosine Hydroxylase antibody produced in mouse
clone TH-2, ascites fluid
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
TH-2, monoclonal
contains
15 mM sodium azide
species reactivity
human, monkey, guinea pig, rat, sheep, bovine, rabbit
technique(s)
immunohistochemistry: suitable
immunoprecipitation (IP): suitable using native or SDS-denatured TH.
western blot: 1:10,000 using extracts of cultured rat adrenal pheochromocytoma (PC12) cells.
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
Monoclonal Anti-Tyrosine Hydroxylase (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Tyrosine hydroxylase (TH) RNA undergoes alternative splicing resulting in four isoforms of TH subunit protein in humans. The four human isoforms are TH-1 (55.6 kDa), TH-2 (56 kDa), TH-3 (58.1 kDa), and TH-4 (58.5 kDa). Only humans express all four isoforms.
Tyrosine hydroxylase (TH) is encoded by the gene mapped to human chromosome 11p15. TH is a tetramer of four identical subunits, which is characterized with a regulatory, catalytic, and tetramerization domains. The enzyme utilizes tyrosine, tetrahydrobiopterin (BH4) and O2 as cosubstrates, and Fe2+ as a cofactor.
Specificity
The antibody recognizes an epitope present in the N-terminal region (approx. aa 9-16) of both rodent and human tyrosine hydroxylase. Clone TH-2 reacts with the intact TH subunits.
Immunogen
rat tyrosine hydroxylase (TH).
Application
Monoclonal Anti-Tyrosine Hydroxylase antibody produced in mouse has also been used in
- western blotting
- indirect immunofluorescence
- immunostaining
- immunohistochemistry
- enzyme linked immunosorbent assay (ELISA)
- dot blot
- immunoprecipitation
Monoclonal Anti-tyrosine hydroxylase antibody produced in mouse has been used in western blotting and immunocytochemistry.
Biochem/physiol Actions
Tyrosine hydroxylase (TH) catalyzes the first rate limiting step in the biosynthesis of catecholamine neurotransmitter i.e. the conversion of L-tyrosine to L-dopa. Inhibition of TH by L-phenylalanine, might play a crucial role in phenylketonuria and block the synthesis of norepinephrine. Activity of TH can be regulated by phosphorylation. Decreased expression of TH is associated with various neuropsychiatric diseases such as schizophrenia and Parkinson′s disease (PD).
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.
recommended
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
Chemical sympathectomy-induced changes in TH-, VIP-, and CGRP-immunoreactive fibers in the rat mandible periosteum: Influence on bone resorption
Cherruau M, et al.
Journal of Cellular Physiology, 194(3), 341-348 (2003)
Essential role of mesolimbic brain-derived neurotrophic factor in chronic social stress-induced depressive behaviors
Koo JW, et al.
Biological Psychiatry, 80(6), 469-478 (2016)
Induction of neurite outgrowth in PC12 cells by the bacterial nucleoside N6-methyldeoxyadenosine is mediated through adenosine A2a receptors and via cAMP and MAPK signaling pathways
Charles MP, et al.
Biochemical and biophysical research communications, 304(4), 795-800 (2003)
Multiple genes on chromosome 7 regulate dopaminergic amacrine cell number in the mouse retina
Whitney IE, et al.
Investigative Ophthalmology & Visual Science, 50(5), 1996-2003 (2009)
Human tyrosine hydroxylase isoforms inhibition by excess tetrahydropterin and unusual behavior of isoform 3 after cAMP-dependent protein kinase phosphorylation
Alterio J, et al.
Test, 273(17), 10196-10201 (1998)
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