Human Resistin ELISA

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Description
Human Resistin ELISA enables the user to determine the exact concentration of Resistin in human serum/plasma as well as other body fluids and thereby assists investigation of Resistin biology.
Documents del producto
Product specifications
| Category | ELISA Kits |
| Reactivity | Human |
| Assay Data | Reference Material: recombinant resistin Incubation Period: 4h Calibrator: recombinant resistin Controlrs: 2 Controls, lyophilised |
| Assay Type | Sandwich |
| Test Range | 0.0121 – 21 µg/L |
| Sensitivity | <0.0121 µg/L |
| Recommended Dilution | 1:21 |
| Origin | Antibody: Rabbit |
| Size 1 | 96 det. |
| Tested Applications | Elisa |
| Sample Type | Serum EDTA / Heparin Plasma |
| Availability | 3-5 days. |
| Storage | Shelf life: between 1 and 2 years Store the kit at 2-8°C after receipt until its expiry date |
| Alias | adipose tissue-specific secretory factor ,ADSF |
| Background | Elisa Kits for: RETN |
| Status | IVD |
| Note | Intra/Interassay Variance [%]<10 |
Descripción
Human Resisitin ELISA kit permite al usuario determinar la concentración exacta de resistina en suero/plasma humano, así como en otros fluidos corporales y, de este modo, ayuda a la investigación de la biología de la resistina.
Resistin, a cysteine-rich protein of 11.3 kDa, was firstly found in mice and constitutes together with RELMα RELMß and RELMγ the protein family of resistin-like molecules (RELM). In humans, resistin and RELMß but no other proteins of the RELM family were found. The human form of resistin shows a homology of 53% to the murine protein. It has 11 cysteineresidues, is synthesized as a propetide of 108 amino acids and secreted as a dimer, build by a disulfide bridge of cysteine residues. Beside this intermolecular disulfide bridge, 5 additional intramolecular ones exist. Appearance of multi- and oligomer formation was proved by size exclusion chromatography. Thereby it was shown, that oligomer formation is SDS-insensitive but can be inhibited by βmercaptoethanol and is therefore likely to be caused by disulfide bridges. Further on, the resistin structure seems to be dependent on its concentration, as circular dichroism analysis shows a concentration dependent shift of α-helical to ß-sheet structure.
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