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Acylated Ghrelin (human) Express ELISA kit

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    Acylated Ghrelin (human) Express ELISA kit
  • Acylated Ghrelin (human) Express ELISA kit
Cat No: A05106
Assays - Ache Kits
SPI-Bio
€440.00
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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Territorial Availability: Available worldwide directly through Bertin Technologies 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
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
Stability: Store at -20degrees; shelf life 2 years maximum after production
Application Media: Plasma, buffer|Blood collection on inhibitor then 1/5 dilution prior assay
Sample volume: 20 µl
Tracer: AcetylCholinesterase AChE
Detection Limit: 0.3pg/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

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

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

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 préproghréline 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 SPI-BIO HUMAN GHRELIN KITS

Vestergaard ET, Jessen N, Moller N, Jorgensen JO. Acyl Ghrelin Induces Insulin Resistance Independently of GH, Cortisol, and Free Fatty Acids. Sci Rep. 2017 Feb 15; 7:42706. doi: 10.1038/srep42706

van Adrichem RC, van der Lely AJ, Huisman M et al. Plasma acylated and plasma unacylated ghrelin: useful new biomarkers in patients with neuroendocrine tumors? Endocr Connect. 2016 Jul;5(4):143-51. doi: 10.1530/EC-16-0021. Epub 2016 May 23

Lauritzen ES, Voss T, Kampmann U et al. Circulating acylghrelin levels are suppressed by insulin and increase in response to hypoglycemia in healthy adult volunteers. Eur J Endocrinol. 2015 Apr;172(4):357-62. doi: 10.1530/EJE-14-0880. Epub 2015 Jan 19

Kanat BH, Ayten R, Aydın S et al. Significance of appetite hormone ghrelin and obestatin levels in the assessment of the severity of acute pancreatitis. Turk J Gastroenterol. 2014 Jun;25(3):309-13. doi: 10.5152/tjg.2014.4081

Delhanty P. et al. The Acylated (AG) to Unacylated (UAG) Ghrelin Ratio in Esterase Inhibitor-Treated Blood Is Higher Than Previously Described. Clin Endocrinol (Oxf). 2015 Jan;82(1):142-6. doi: 10.1111/cen.12489. Epub 2014 Jun 2

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. doi: 10.1186/s13023-016-0440-0

Kuppens RJ, Diène G, Bakker NE et al. Elevated ratio of acylated to unacylated ghrelin in children and young adults with Prader-Willi syndrome. Endocrine. 2015 Dec;50(3):633-42. doi: 10.1007/s12020-015-0614-x. Epub 2015 May 20

Homann D. et al. Hyperleptinemia independent of body adiposity in women with fibromyalgia. Rheumatol Int (2014) DOI 10.1007/s00296-014-2988-0

Wasse L. et al. The influence of vigorous running and cycling exercise on hunger perceptions and plasma acylated ghrelin concentrations in lean young men. Appl. Physiol. Nutr. Metab.(2013) dx.doi.org/10.1139/apnm-2012-0154

Gungor S. et al. Ghrelins, obestatin, nesfatin-1 and leptin levels in pregnant women with 2 and without hyperemesis gravidarum. Clin Biochem. (2013) DOI: 10.1016/j.clinbiochem.2013.01.015

Broom D. et al. Influence of resistance and aerobic exercise on hunger, circulating levels of acylated ghrelin, and peptide YY in healthy males. Am J Physiol Regulatory Integrative Comp Physiol (2009) doi:10.1152/ajpregu.90706.2008

Broom D. et al. Exercise-induced suppression of acylated ghrelin in humans. J Appl Physiol (2007) doi:10.1152/japplphysiol.00759.2006

Lee Y. et al. Lupin-enriched bread increases satiety and reduces energy intake acutely. Am J Clin Nutr (2006) doi: 10.3945/ ajcn.2008.26708

Cederberg H. et al. Unacylated ghrelin is associated with changes in body composition and body fat distribution during long-term exercise intervention. European Journal of Endocrinology (2011) DOI: 10.1530/EJE-11-0334

SPI-Bio is a brand name of Bertin Bioreagent.
Bertin Bioreagent includes over 100 employees, chemists, biochemists, immunoanalysts, pharmacists and technicians.
Always at the forefront of innovation and after launching on the market products incorporating in their time innovative technologies (Acetylcholinesterase tracer for EIA), this brand offers a wide and unique range of assays for biomarker Immunoassays (SPI-Bio TM) thanks to a solid knowledge acquired during the last 25 years in developping over 100 biomarkers assays.

To better serve you, we aim to design our products and reagents to address your needs on the expected performance in terms of a possible range of use, but also on operational conditions of use & regulations.
Thanks to our production processes and quality controls, we provide you with products with compliance to specifications.
Our technical support & science teams are available to help you assess their relevance depending on your needs, to specify the conditions of application and their fields of use. Finally, our researchers are ready to provide you with the necessary support by going, if needed, in your laboratories to validate your operating conditions and to solve possible problems.

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