SAB4200218
Anti-Glycogen Synthase 1 (N-terminal) antibody produced in rabbit
~1.5 mg/mL, affinity isolated antibody
Synonym(s):
Anti-GYS1, Anti-Glycogen synthase 1 (muscle)
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Pricing and availability is not currently available.
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~84 kDa
species reactivity
mouse, rat
concentration
~1.5 mg/mL
technique(s)
immunoprecipitation (IP): 5-10 μg using rat brain extracts (S1 fraction)
indirect immunofluorescence: 5-10 μg/mL using NIH3T3 cells
western blot: 1.5-3 μg/mL using mouse brain extracts (S1 fraction)
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GYS1(2997)
General description
The glycogen synthase 1 (GYS1) gene is mapped to human chromosome 19q13.3. In mammals, two glycogen synthase (GS) isoforms have been identified, the muscle GS form, glycogen synthase 1 (GYS1) and the liver specific form, glycogen synthase 2 (GYS2, LGS). GYS1 is predominantly expressed in the skeletal and cardiac muscles.
Specificity
Anti-Glycogen Synthase 1 (N-terminal), specifically recognizes mouse and rat glycogen synthase 1.
Application
Anti-Glycogen Synthase 1 (N-terminal) antibody produced in rabbit is suitable for:
- immunoblotting
- immunoprecipitation
- immunofluorescence
Biochem/physiol Actions
Glycogen synthase (GS or GYS), the rate-limiting enzyme for glycogen biosynthesis, catalyzes the incorporation of α-1,4-linked glucose units into glycogen chains. Both, the muscle (GYS1) and the liver GS (GYS2) forms are highly regulated by phosphorylation, glucose availability, glycogen levels and allosteric effectors. In response to hormonal stimuli, GS is phosphorylated on up to nine serine residues resulting in progressive inactivation of the two isoforms. GS activity is stimulated by insulin in liver, muscle and adipose tissues. The enzyme undergoes dephosphorylation allosteric activation and thus translocates between various subcellular compartments. Insulin increases GS activity primarily by dephosphorylation of four key residues, a process thought to be mediated by the activation of protein phosphatase-1 (PP1) and the inactivation of glycogen synthase kinase-3 (GSK3). GYS1 deficiency might lead to congenital disorders associated with glycogen metabolism.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
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 Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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T C Jensen et al.
The Journal of biological chemistry, 275(51), 40148-40154 (2000-10-03)
A protocol was developed in 3T3-L1 adipocytes that resulted in the specific desensitization of glycogen synthase activation by insulin. Cells were pretreated for 15 min with 100 nm insulin, and then recovered for 1.5 h in the absence of hormone.
María M Adeva-Andany et al.
BBA clinical, 5, 85-100 (2016-04-07)
In the human body, glycogen is a branched polymer of glucose stored mainly in the liver and the skeletal muscle that supplies glucose to the blood stream during fasting periods and to the muscle cells during muscle contraction. Glycogen has
Juan C Ferrer et al.
FEBS letters, 546(1), 127-132 (2003-06-28)
Traditionally, glycogen synthase (GS) has been considered to catalyze the key step of glycogen synthesis and to exercise most of the control over this metabolic pathway. However, recent advances have shown that other factors must be considered. Moreover, the control
Alexander von Wilamowitz-Moellendorff et al.
Diabetes, 62(12), 4070-4082 (2013-08-31)
The liver responds to an increase in blood glucose levels in the postprandial state by uptake of glucose and conversion to glycogen. Liver glycogen synthase (GYS2), a key enzyme in glycogen synthesis, is controlled by a complex interplay between the
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