Nori Equine BMP2 ELISA Kit
$461.00 – $832.00
This ELISA kit is for quantification of BMP2 in equine. This is a quick ELISA assay that reduces time to 50% compared to the conventional method, and the entire assay only takes 3 hours. This assay employs the quantitative sandwich enzyme immunoassay technique and uses biotin-streptavidin chemistry to improve the performance of the assays. An antibody specific for BMP2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any BMP2 present is bound by the immobilized antibody. After washing away any unbound substances, a detection antibody specific for BMP2 is added to the wells. Following wash to remove any unbound antibody reagent, a detection reagent is added. After intensive wash a substrate solution is added to the wells and color develops in proportion to the amount of BMP2 bound in the initial step. The color development is stopped, and the intensity of the color is measured.
Alternative names for BMP2: Bone morphogenetic protein 2, BMP-2
This product is for Laboratory Research Use Only not for diagnostic and therapeutic purposes or any other purposes.
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Description
Nori Equine BMP2 ELISA Kit Summary
Alternative names for BMP2: Bone morphogenetic protein 2, BMP-2
Alternative name for equine: horse
| Assay Type | Solid Phase Sandwich ELISA |
| Format | 96-well Microplate or 96-Well Strip Microplate |
| Method of Detection | Colorimetric |
| Number of Targets Detected | 1 |
| Target Antigen Accession Number | F6T889 |
| Assay Length | 3 hours |
| Quantitative/Semiquantitative | Quantitative |
| Sample Type | Plasma, Serum, Cell Culture, Urine, Cell/Tissue Lysates, Synovial Fluid, BAL, |
| Recommended Sample Dilution (Plasma/Serum) | No dilution for sample <ULOQ; sufficient dilution for samples >ULOQ |
| Sensitivity | 9 pg/mL |
| Detection Range | 46.9-3000 pg/mL |
| Specificity | Equine BMP2 |
| Cross-Reactivity | < 0.5% cross-reactivity observed with available related molecules, < 50% cross-species reactivity observed with species tested. |
| Interference | No significant interference observed with available related molecules |
| Storage/Stability | 4 ºC for up to 6 months |
| Usage | For Laboratory Research Use Only. Not for diagnostic or therapeutic use. |
| Additional Notes | The kit allows for use in multiple experiments. |
Standard Curve
Kit Components
1. Pre-coated 96-well Microplate
2. Biotinylated Detection Antibody
3. Streptavidin-HRP Conjugate
4. Lyophilized Standards
5. TMB One-Step Substrate
6. Stop Solution
7. 20 x PBS
8. Assay Buffer
Other Materials Required but not Provided:
1. Microplate Reader capable of measuring absorption at 450 nm
2. Log-log graph paper or computer and software for ELISA data analysis
3. Precision pipettes (1-1000 µl)
4. Multi-channel pipettes (300 µl)
5. Distilled or deionized water
Protocol Outline
1. Prepare all reagents, samples and standards as instructed in the datasheet.
2. Add 100 µl of Standard or samples to each well and incubate 1 h at RT.
3. Add 100 µl of Working Detection Antibody to each well and incubate 1 h at RT.
4. Add 100 µl of Working Streptavidin-HRP to each well and incubate 20 min at RT.
5. Add 100 µl of Substrate to each well and incubate 5-30 min at RT.
6. Add 50 µl of Stop Solution to each well and read at 450 nm immediately.
Background:
Bone morphogenetic protein 2 (BMP-2) belongs to the TGF-β superfamily of proteins (1). BMP-2 has been shown to interact with BMPR1A. Like other bone morphogenetic proteins BMP-2 plays an important role in the development of bone and cartilage (2). It is involved in the hedgehog pathway, TGF beta signaling pathway, and in cytokine-cytokine receptor interaction. It is also involved in cardiac cell differentiation and epithelial to mesenchymal transition. BMP-2 and BMP-7 are osteo-inductive BMPs: they have been demonstrated to potently induce osteoblast differentiation in a variety of cell types (3).
References
- Sampath TK, et al. (5 August 1990). J. Biol. Chem. 265 (22): 13198
- Chen D, et al. (December 2004). Growth Factors 22 (4): 233
- Marie PJ, et al. (2002). Histol. Histopathol. 17 (3): 877
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