| Weight | 1 lbs |
|---|---|
| Dimensions | 9 × 5 × 2 in |
| host | chicken |
| isotype | IgY |
| clonality | polyclonal |
| concentration | 1 mg/mL |
| applications | ICC/IF, IHC, WB |
| reactivity | tagged fusion proteins |
| available sizes | 1 mg, 100 µg, 25 µg |
chicken anti-mCherry polyclonal antibody 1514
$100.00 – $2,600.00
Antibody summary
- Chicken polyclonal to mCherry
- Suitable for: WB, ICC/IF, IHC
- Reacts with: tagged fusion proteins
- Isotype: IgY
- 100 µg, 25 µg, 1 mg
chicken anti-mCherry polyclonal antibody 1514
| target relevance |
|---|
| Protein expression of mCherry and mCherry tagged proteins can be checked and quantified using this antibody in Western blotting. When imaging in situ, mCherry fluorescence can be amplified by this antibody when used in conjunction with a suitable fluorescent label or secondary antibody. Click for more on: epitope tags and mCherry |
| Biotechnology mCherry, a widely used fluorescent protein, has become an indispensable tool in various areas of scientific research. Derived from the red fluorescent protein DsRed, mCherry emits bright red fluorescence when excited with green light, making it an excellent choice for fluorescence microscopy and live-cell imaging studies. Researchers commonly utilize mCherry as a reporter gene, allowing them to track and visualize specific proteins, organelles, or cellular structures in real-time within living cells and organisms. Its compatibility with other fluorescent proteins enables dual-labeling experiments and multiplexing, providing valuable insights into dynamic cellular processes and interactions. Additionally, mCherry???s stability and resistance to photobleaching enhance its utility for long-term imaging studies. Moreover, mCherry has been employed in various fields, including cell biology, molecular biology, neuroscience, and developmental biology, where its fluorescence serves as a powerful tool to investigate cellular behavior, protein localization, and gene expression patterns. As research methodologies continue to advance, mCherry???s versatility and reliability continue to contribute significantly to our understanding of complex biological phenomena and pave the way for new discoveries in the life sciences. |
Data
 |
| HEK293 cells transfected with a mCherry, stained with 1514 antibody and viewed in a confocal microscope. Most HEK293 cells are not transfected so only the nucleus of these cells can be visualized with a blue DNA stain. Cells which are transfected with mCherry are bright red, and staining with 1514 is shown in Green. The green antibody staining is only seen cells which express mCherry, as expected, and the superimposition of the green and red results in an orange signal. Interestingly stronger mCherry staining is seen in the nucleus, possibly due to degradation of some mCherry molecules releasing the low molecular weight mCherry fluorochrome. |
 |
| Chromogenic immunostaining of formalin fixed paraffin embedded tissue from a mouse transgenically expressing a Cre dependent oxytocin-Tdtomato construct in brain tissue. TdTomato is very closely related to mCherry, so 1514 recognizes both proteins. The 1514 antibody was used at a dilution 1:10,000, detected in DAB (brown) following the 8718C method and citra buffer heat retrieval. Hematoxylin (blue) was used as the counterstain. The 1514 specifically detects as expected the soma and axons of Cre expressing neurons. |
 |
| Western blot analysis of HEK293 cell lysates using chicken pAb to mCherry, 1514, dilution 1:2,000, in green, and rabbit pAb to GAPDH, 574, dilution 1:5,000, in red: [1] protein molecular weight standard, [2] untransfected HEK293 control cells, [3] HEK293 cells transfected with pCI-Neo-mod vector expressing two tdTomato protein domains, [4] HEK293 cells transfected with pCI-Neo-mod vector expressing one mCherry-HA protein domain, and [5] HEK293 cells transfected with pCI-Neo-mod vector expressing one GFP domain. The 1514 antibody recognizes tdTomato and mCherry proteins revealing major bands at about 60kDa and 30kDa, but does not recognize GFP. The red band at 37kDa corresponds to GAPDH protein here used as a loading control. |
Publications
Publications
| pmid | title | authors | citation |
|---|---|---|---|
| 15558047 | Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. | Nathan C Shaner, Robert E Campbell, Paul A Steinbach, Ben N G Giepmans, Amy E Palmer, Roger Y Tsien | Nat Biotechnol 22:1567-72 |
| 11050231 | Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine). | A A Heikal, S T Hess, G S Baird, R Y Tsien, W W Webb | Proc Natl Acad Sci U S A 97:11996-2001 |
| 11050230 | The structure of the chromophore within DsRed, a red fluorescent protein from coral. | L A Gross, G S Baird, R C Hoffman, K K Baldridge, R Y Tsien | Proc Natl Acad Sci U S A 97:11990-5 |
| 11050229 | Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. | G S Baird, D A Zacharias, R Y Tsien | Proc Natl Acad Sci U S A 97:11984-9 |
Protocols
| relevant to this product |
|---|
| Western blot IHC ICC |
Documents
| # | SDS | Certificate | |
|---|---|---|---|
| Please enter your product and batch number here to retrieve product datasheet, SDS, and QC information. | |||
