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G8751

Sigma-Aldrich

Glycogen from oyster

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352201
NACRES:
NA.25

InChI

1S/C24H42O21/c25-1-5-9(28)11(30)16(35)22(41-5)39-4-8-20(45-23-17(36)12(31)10(29)6(2-26)42-23)14(33)18(37)24(43-8)44-19-7(3-27)40-21(38)15(34)13(19)32/h5-38H,1-4H2/t5-,6-,7-,8-,9-,10-,11+,12+,13-,14-,15-,16-,17-,18-,19-,20-,21+,22+,23-,24-/m1/s1

InChI key

BYSGBSNPRWKUQH-UJDJLXLFSA-N

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General description

Glycogen is a branched polymer of glucose synthesized by animal cells for energy storage and release. It is constructed of predominantly α1→4 glycosidic bonds with branches created through α1→6 glycosidic bonds.
Glycogen, a polysaccharide of glucose, serves as the primary storage of glucose in the body and functions as a vital energy reserve in both fungi and animals. With its multibranched structure, glycogen is a secondary long-term energy storage molecule, similar to starch, and closely related to amylopectin, playing a pivotal role in energy storage and release and existing as granules in the cytoplasm.
In research, glycogen is commonly employed to investigate carbohydrate storage, metabolism, and enzyme characterization. Serving as an inert carrier, it significantly enhances the efficiency of DNA and RNA extraction through ethanol precipitation. Its versatility proves valuable in unraveling the intricate details of the glucose cycle, contributing to advancements in diverse areas of physiological, nutritional, biochemical, and cell biology research.
The Pacific oyster/Crassostrea gigas is a vital marine fishery resource. 20-40% of the dry weight of an oyster accounts for glycogen. High levels of glycogen contribute to the flavor, quality, and hardiness of the oyster.

Application

Glycogen from oyster has been used:
  • as a component in acrylamide slab gels to perform branching enzyme activity staining for quantifying ADP-glucose pyrophosphorylase (AGPase) activity
  • as a sterile inflammatory agent for inoculating into mice for obtaining peritoneal exudate cells (PEC) and to study its effects on the metabolic functions of macrophages
  • as a primer for supplementing maleate buffer for amylosucrase assay to measure the activities of the glutathione S-transferase (GST-AS) amylosucrase fusion protein and the purification fractions
  • as a supplement in PreScission buffer to perform polymer synthesis reaction

Oyster glycogen has been used to induce inflammation and to promote extravasation of granulocytes and neutrophils in animal models after intraperitoneal injection. Glycogen also acts as a vascular permeability probe.

Features and Benefits

  • Ideal for Biochemical and Cell Biology research
  • Versatile and adaptable for wide variety of laboratory and research applications

Other Notes

For additional information on our range of Biochemicals, please complete this form.
To gain a comprehensive understanding of our extensive range of Polysaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Busu Li et al.
BMC genomics, 18(1), 713-713 (2017-09-13)
The Pacific oyster Crassostrea gigas is an important marine fishery resource, which contains high levels of glycogen that contributes to the flavor and the quality of the oyster. However, little is known about the molecular and chemical mechanisms underlying glycogen
Henrik U Irgens et al.
The Journal of clinical endocrinology and metabolism, 100(5), E767-E775 (2015-03-10)
The synthesis of glycogen is initiated by glycogenin. In humans, glycogenin-1 is expressed ubiquitously, whereas glycogenin-2 (GN2) is highly expressed in liver. It has therefore been suggested that GN2 is a liver isoform of glycogenin. In a search for possible
G P De Montalk et al.
Journal of bacteriology, 181(2), 375-381 (1999-01-12)
The Neisseria polysaccharea gene encoding amylosucrase was subcloned and expressed in Escherichia coli. Sequencing revealed that the deduced amino acid sequence differs significantly from that previously published. Comparison of the sequence with that of enzymes of the alpha-amylase family predicted
Hiroki Asai et al.
Journal of experimental botany, 65(18), 5497-5507 (2014-07-30)
Starch synthase (SS) IIIa has the second highest activity of the total soluble SS activity in developing rice endosperm. Branching enzyme (BE) IIb is the major BE isozyme, and is strongly expressed in developing rice endosperm. A mutant (ss3a/be2b) was
Naoko Fujita et al.
Journal of experimental botany, 62(14), 4819-4831 (2011-07-07)
Starch synthase (SS) I and IIIa are the first and second largest components of total soluble SS activity, respectively, in developing japonica rice (Oryza sativa L.) endosperm. To elucidate the distinct and overlapping functions of these enzymes, double mutants were

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