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mouse anti-mCherry monoclonal antibody (5B1) 4068


Antibody summary

  • Mouse monoclonal to mCherry
  • Suitable for: WB, ICC/IF, IHC
  • Reacts with: tagged fusion proteins
  • Isotype: IgG2a
  • 100 µg, 25 µg, 1 mg
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SKU: 4068parent Categories: , Tags: ,
Weight1 lbs
Dimensions9 × 5 × 2 in







1 mg/mL



available sizes

1 mg, 100 µg, 25 µg

Database link:
mCherry X5DSL3
Tested applications
Recommended dilutions
WB: 1:2000 IF/IHC: 1:500
Full length recombinant protein
Size and concentration
25, 100, 1000µg and 1 mg/mL
Storage Instructions
2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Storage buffer
PBS, 50% glycerol, 0.04% NaN3
affinity purified
Compatible secondaries
goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 5486
goat anti-mouse IgG, H&L chain specific, biotin conjugated, Conjugate polyclonal antibody 2685
goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody 7854
goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1706
goat anti-mouse IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1716
goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1721
Isotype control
Mouse monocolonal IgG2a - Isotype Control
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
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.


No results found


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

13911999Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, AequoreaSHIMOMURA O, JOHNSON FH, SAIGA Y.J Cell Comp Physiol. 1962 Jun;59:223-39. doi: 10.1002/jcp.1030590302.
12693991A colourless green fluorescent protein homologue from the non-fluorescent hydromedusa Aequorea coerulescens and its fluorescent mutantsGurskaya NG, Fradkov AF, Pounkova NI, Staroverov DB, Bulina ME, Yanushevich YG, Labas YA, Lukyanov S, Lukyanov KA.Biochem J. 2003 Jul 15;373(Pt 2):403-8. doi: 10.1042/BJ20021966.
11988576Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cellsZacharias DA, Violin JD, Newton AC, Tsien RY.Science. 2002 May 3;296(5569):913-6. doi: 10.1126/science.1068539.
9759496The green fluorescent proteinTsien RY.Annu Rev Biochem. 1998;67:509-44. doi: 10.1146/annurev.biochem.67.1.509.
8703075Crystal structure of the Aequorea victoria green fluorescent proteinOrmö M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ.Science. 1996 Sep 6;273(5280):1392-5. doi: 10.1126/science.273.5280.1392.
8448132Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent proteinCody CW, Prasher DC, Westler WM, Prendergast FG, Ward WW.Biochemistry. 1993 Feb 9;32(5):1212-8. doi: 10.1021/bi00056a003.
8303295Green fluorescent protein as a marker for gene expressionChalfie M, Tu Y, Euskirchen G, Ward WW, Prasher DC.Science. 1994 Feb 11;263(5148):802-5. doi: 10.1126/science.8303295.
7809066Wavelength mutations and posttranslational autoxidation of green fluorescent proteinHeim R, Prasher DC, Tsien RY.Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12501-4. doi: 10.1073/pnas.91.26.12501.
1347277Primary structure of the Aequorea victoria green-fluorescent proteinPrasher DC, Eckenrode VK, Ward WW, Prendergast FG, Cormier MJ.Gene. 1992 Feb 15;111(2):229-33. doi: 10.1016/0378-1119(92)90691-h.


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Western blot


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