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Unacylated Ghrelin (mouse, rat) Express ELISA kit

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    Unacylated Ghrelin (mouse, rat) Express ELISA kit
  • Unacylated Ghrelin (mouse, rat) Express ELISA kit
Cat No: A05118
Assay Kits - Elisa
Bertin Bioreagent
€453.00
Price is excluding VAT and does not include packaging neither shipping

Enzyme ImmunoAssay (EIA) is a technique to detect and quantify antigens (proteins, hormones…) or antibodies in samples. It relies on the ability of an antibody to bind a specific antigen. Either the antibody or the antigen is labelled with an enzyme wh...

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: 96 wells

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Territorial Availability: Available worldwide directly through Bertin or your local distributor
Technical Warning: Check the Additional Items Required section of this kit booklet to verify if UltraPure Water (Milli-Q or equivalent) is needed for this assay
Synonyms:
  • Unacylated Ghrelin (rat/mouse) EIA kit
  • Des-octanoyl Ghrelin
Correlated keywords:
  • ELISA
  • spi-bio
  • acylated
  • immunoassays
  • obesity
  • growth
  • hormones
  • homeostasis
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Product Overview:
Enzyme ImmunoAssay (EIA) is a technique to detect and quantify antigens (proteins, hormones…) or antibodies in samples. It relies on the ability of an antibody to bind a specific antigen. Either the antibody or the antigen is labelled with an enzyme whose substrate is a chromogen or a fluorogen converted in a measurable product (color or fluorescence).
Enzyme-linked Immunosorbent Assay (ELISA) is a type of EIA using a solid phase (ex: microtiter plate) coated with an antigen immobilizing the molecule to detect. Over the time, scientists have extended the term ELISA to EIAs using an antibody coating the solid phase. That explains why our EIA kits using coated antibodies are also called ELISA kits.
Bertin Bioreagent’s expertise is to develop analytical tools for biomarkers. As such, in 2004, Bertin Bioreagent launched its first Ghrelin Biomarker assay kits, under the SPI-Bio brand name, as a result of its state-of-the-art R&D research teams. Bertin Bioreagent was the first company providing bioanalytical tools to assay Acylated and Non-acylated Ghrelin with very high sensitivity.
Ghrelin discovered in 1999, is fast becoming an endocrinology target of the millennium. Ghrelin, identified in rat stomach as an endogenous ligand for the GH secretagogue receptor, is mainly produced in stomach, but has been demonstrated in many other organs. In addition to GH-releasing properties and its orexant action, ghrelin could act as an hormone having effects on gastric motility (similarity with the peptide hormone motilin), acidic secretion, cardiovascular action, antiproliferative effects, pancreatic and glucose metabolism function, sleep... Ghrelin gene raises to mRNA prepro-ghrelin of 117 amino acids. This precursor is processed into ghrelin, 28 amino acids (human). Before being secreted, this peptide is octanoylated at Ser 3. This step is essential for biological activity. If the endogenous peptide appears directly related to feeding behaviour, the potential therapeutic importance of this hormone is not restricted to a regulator of food intake but also may be involved osteoporosis somatopaus, infertility and ovulation induction, and some cardiovascular diseases.
Size 96 wells
Shipping wet ice
Specificity
Application Media Plasma, buffer|Blood collection on inhibitor then 1/10 dilution prior assay
Sample volume 10 µL
Tracer AcetylCholinesterase AChE
Detection Limit 0.6 pg/mL
Standard Curve Range 2-250 pg/mL
Custom Code 3822000000
UNSPSC code 41116104

PRODUCT EXPLANATION: ACETYLCHOLINESTERASE MARKER IN ENZYME-IMMUNOASSAYS

Grassi J., Pradelles P. Compounds labelled by the acetylcholinesterase of Electrophorus Electricus. Its preparation process and its use as a tracer or marquer in enzymo-immunological determinations. United States patent, N° 1,047,330. September 10, 1991

Grassi J., Pradelles P. The use of Acetylcholinesterase as a Universal marker in Enzyme-Immunoassays. Proceedings of the Third International Meeting on Cholinesterases, American Chemical Society (1991)

Pradelles P., Grassi J., Maclouf J. Enzyme Immunoassays of Eicosanoids Using Acetylcholinesterase. Methods in Enzymology (1990), vol. 187, 24-34

PRODUCT EXPLANATION: GHRELIN

Kojima M, Kangawa K. Ghrelin: structure and function. Physiol. Rev ( 2005), 85:495-522

Müller TD, Nogueiras R, Andermann ML et al. Ghrelin. Mol Metab. 2015 Mar 21;4(6):437-60

Bluet-Pajot MT, Tolle V, Zizzari P, Tomasetto C, Grouselle D, Epelbaum J. Ghrelin: A striking example of neuroendocrine peptide pleiotropy. Med Sci (Paris), August 1, 2005, 21 (8-9): 715-21

de Faria Barros A et al. Is there association between acyl-ghrelin and inflammation in hemodialysis patients? J Bras Nefrol. (2013) 35(2):120-126

Grousselle D et al. Variations des peptides dérivés de la pr?proghréline au cours du repas dans l?anorexie mentale restrictive. Poster GIR-AFDAS-TCA2014

Delhanty P et al. Des-acyl ghrelin analogs prevent high-fat-diet-induced dysregulation of glucose homeostasis. FASEB J. (2013) 27(4):1690-1700

Costantini, V et al. GSK1614343, a Novel Ghrelin Receptor Antagonist, Produces an Unexpected Increase of Food Intake and Body Weight in Rodents and Dogs. Neuroendocrinology (2011);94:158–168

Porporato E, Filigheddu N et al. Acylated and unAcylated Ghrelin impair skeletal muscle atrophy in mice. J. Clinical Invest (2013) 123(2): 611-622

Sentissi O, Epelbaum J, Olié JP, Poirier MF. Leptin and Ghrelin Levels in Patients With Schizophrenia During Different Antipsychotics Treatment: A Review. Schizophrenia Bulletin (2008) 34(6), 1189–1199

PRODUCT EXPLANATION: KIT VALIDATION

Valentin MA, Ma S, Zhao A, Legay F, Avrameas A. Validation of immunoassay for protein biomarkers: Bioanalytical study plan implementation to support pre-clinical and clinical studies. J Pharm Biomed Anal. (2011) 55(5) : 869-877

European Medicines Agency. Guideline on bioanalytical method validation, 21 July 2011

CITATIONS OF GHRELIN KITS

Hassouna, Grouselle D, Chiappetta G et al. Combination of Selective Immunoassays and Mass Spectrometry to Characterize Preproghrelin-Derived Peptides in Mouse Tissues. Front Neurosci. 2017 Apr 20;11:211

Beauloye V, Diene G, Kuppens R et al. High unacylated ghrelin levels support the concept of anorexia in infants with prader-willi syndrome. Orphanet J Rare Dis. 2016 May 4;11(1):56

Erden I, Uçak H, Demir B et al. Serum ghrelin levels in patients with Behcet's disease.Postepy Dermatol Alergol. 2016 Dec;33(6):450-456

Gagnon J, Anini Y. Insulin and Norepinephrine Regulate Ghrelin Secretion from a Rat Primary Stomach Cell Culture. Endocrinology (2012) doi 10.1210/en.2012-1040

Lin Li R, Sherbet D et al. Profound Hypoglycemia in Starved, Ghrelin-deficient Mice Is Caused by Decreased Gluconeogenesis and Reversed by Lactate or Fatty Acids. JBC (2012)

Lu X et al. Postprandial inhibition of gastric ghrelin secretion by long-chain fatty acid through GPR120 in isolated gastric ghrelin cells and mice. Am J Physiol Gastrointest Liver Physiol (2012)doi:10.1152/ajpgi.00541.2011

Robert F et al. Targeting Protein Synthesis in a Myc/mTOR-Driven Model of Anorexia-Cachexia Syndrome Delays Its Onset and Prolongs Survival. Cancer Res (2012) doi:10.1158/0008-5472.CAN-11-2739

Teubner B et al. Inhibition of ghrelin O-acyltransferase attenuates food deprivation-induced increases in ingestive behavior. Hormones and Behavior (2013)

Zhao TJ, Liang G et al. Ghrelin O-acyltransferase (GOAT) is essential for growth hormone-mediated survival of calorierestricted mice. PNAS (2010) doi: 10.1073/pnas.1002271107

Zhao TJ, Sakata I et al. Ghrelin secretion stimulated by β1-adrenergic receptors in cultured ghrelinoma cells and in fasted mice. PNAS (2010) doi: doi: 10.1073/pnas.1011116107

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