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- Acylated Ghrelin (pig) ELISA kit
Acylated Ghrelin (pig) ELISA kit
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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 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:
- Acylated Ghrelin (pig) EIA kit
- Octanoyl Ghrelin
Correlated keywords:
- ELISA
- spi-bio
- acylated
- immunoassays
- obesity
- growth
- hormones
- homeostasis
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.
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 dilution prior assay |
| Tracer | AcetylCholinesterase AChE |
| Detection Limit | refer to technical booklet |
| Standard Curve Range | 3,9-500 pg/mL |
| Custom Code | 3822000000 |
| UNSPSC code | 41116104 |
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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.
CITATION OF SPI-BIO PIG GHRELIN KITS
Batorek N., Vogrin Bracic M., Skorjanc D. Serum Concentrations of Leptin, Ghrelin and Cortisol are not Direct Related to the Loss of Backfat Thickness, Body Weight, Protein and Fat at Weaning of Second Parity of Crossbreed Sows (Landrace x Large white). Journal of Animal and Veterinary Advances (2013) 12(6): 766-774
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