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Manufactured by BioVendor

Ganglioside GM2 Activator Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Cerebroside sulfate activator protein, GM2-AP, Shingolipid activator protein 3, SAP-3, GM2AP
  • Species:Human
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Cat. No. Size Price


RD191309200R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Urine, Plasma (EDTA, citrate, heparin)

Sample Requirements

20 µl/well

Storage/Expiration

Store the complete kit at 2 8°C. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

0.16 – 5 ng/ml

Limit of Detection

0.04 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 5.7 %

Inter-assay (Run-to-Run)

n = 7; CV = 7.9 %

Spiking Recovery

96.4 %

Dilutation Linearity

103.6 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 4 hours
  • The kit measures GM2AP in serum, plasma (EDTA, citrate, heparin) and urine
  • Assay format is 96 wells
  • Standard is recombinant protein based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Diabetology - Other Relevant Products, Energy metabolism and body weight regulation, Metabolic syndrome, Neural tissue markers

Summary

Ganglioside GM2 activator protein (GM2AP) is product of the GM2A gene and consists of 170 amino acids. It is a small (20 kDa), heat stable, long-lived, protease-resistant glycosylated protein that normally resides in the lysozome.
GM2AP is an essential cofactor to β-hexosaminidase A (Hex A) in the degradation of GM2 ganglioside to GM3 form. The protein mediates the interaction between the water-soluble exohydrolase and its membrane-embedded glycolipid substrate at the lipid–water interface. It also acts as a lipid transfer protein.
Because of the presence of an N-terminal signal peptide, N-linked glycosylation, and disulfide bonds, it is clear that the activator is synthesized in the endoplasmic reticulum. The protein is first synthesized as a precursor which is then glycosylated, modified, and cleaved at 32Ser to the mature form. GM2AP contains at least three functional elements: a hydrophobic β-cup structure forming a spacious hydrophobic cavity, an oligosaccharide binding site, and an area that interacts with alpha subunit of HexA.
Butkus and Coghlan revealed by northern analysis that GM2AP mRNA has a widespread distribution in ovine tissue. In the kidney, GM2 was expressed in all major renal arteries and arterioles. In the liver, the expression of the gene was prominent in the hepatic vein and duct. Antibodies raised against the GM2AP confirmed that the protein is present at the same sites as the mRNA.
A deficiency of the GM2AP due to a mutation in respective gene can lead to the accumulation of GM2 in the lysosomes of primarily neuronal cells, where the synthesis of the more complex gangliosides is the greatest. This storage leads to neuronal cell death and one of three similar neurodegenerative diseases collectively known as GM2 gangliosidosis. On the other hand, up-regulation of GM2AP expression by oxidized LDL enhances ganglioside accumulation in the aorta, which may be strongly associated with atherosclerosis. Highashi et al observed that administration of GM2AP to mice significantly increased serum insulin levels and blockage of GM2AP function by specific antibodies inhibited insulin secretion. They also observed higher concentration of GM2AP in human serum of obese subjects by ELISA.

Areas of investigation:

  • Diabetology
  • Metabolic syndrome
  • CNS disorders
References to Summary

References to Ganglioside GM2 Activator

  • Butkus A, Coghlan JP. Location of ganglioside GM2 activator protein gene expression in sheep. Clin Exp Pharmacol Physiol Sup. 1998 Nov;25:S28-33
  • Higashi K, Kubo H, Watanabe H, Fujimori K, Mikami T, Kaneko H. Adipokine ganglioside GM2 activator protein stimulates insulin secretion. FEBS Lett. 2011 Aug 19;585 (16):2587-91
  • Higashi K, Mikami T, Yamada T, Kawashima H, Kimura T, Kaneko H. A novel adipokine GM2AP impairs insulin signaling. Biochem Biophys Res Commun. 2010 Nov 19;402 (3):571-6
  • Kolter T, Sandhoff K. Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu Rev Cell Dev Biol. 2005;21:81-103
  • Mathias JD, Ran Y, Carter JD, Fanucci GE. Interactions of the GM2 activator protein with phosphatidylcholine bilayers: a site-directed spin-labeling power saturation study. Biophys J. 2009 Sep 2;97 (5):1436-44
  • Ran Y, Fanucci GE. Ligand extraction properties of the GM2 activator protein and its interactions with lipid vesicles. Biophys J. 2009 Jul 8;97 (1):257-66
  • Rigat B, Yeger H, Shehnaz D, Mahuran D. GM2 activator protein inhibits platelet activating factor signaling in rats. Biochem Biophys Res Commun. 2009 Aug 7;385 (4):576-80
  • Sinici I, Yonekawa S, Tkachyova I, Gray SJ, Samulski RJ, Wakarchuk W, Mark BL, Mahuran DJ. In cellulo examination of a beta-alpha hybrid construct of beta-hexosaminidase A subunits, reported to interact with the GM2 activator protein and hydrolyze GM2 ganglioside. PLoS One. 2013;8 (3):e57908
  • Wendeler M, Werth N, Maier T, Schwarzmann G, Kolter T, Schoeniger M, Hoffmann D, Lemm T, Saenger W, Sandhoff K. The enzyme-binding region of human GM2-activator protein. FEBS J. 2006 Mar;273 (5):982-91
  • Wright CS, Li SC, Rastinejad F. Crystal structure of human GM2-activator protein with a novel beta-cup topology. J Mol Biol. 2000 Dec 1;304 (3):411-22
  • Yanai H, Yoshida H, Tomono Y, Tada N, Chiba H. The possible contribution of a general glycosphingolipid transporter, GM2 activator protein, to atherosclerosis. J Atheroscler Thromb. 2006 Dec;13 (6):281-5
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