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goat anti-mCherry polyclonal antibody 1536


Antibody summary

  • Goat polyclonal to mCherry
  • Suitable for: WB, ICC/IF, IHC
  • Reacts with: tagged fusion proteins
  • Isotype: IgY
  • 100 µg, 25 µg, 1 mg
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SKU: 1536parent 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/ICC 1:1000
Full length recombinant mCherry protein expressed in and purified from E. coli
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
donkey anti-goat IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 1689
donkey anti-goat IgG, H&L chain specific, biotin conjugated polyclonal antibody 1699
donkey anti-goat IgG, H&L chain specific, FITC conjugated polyclonal antibody 1704
donkey anti-goat IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1709
donkey anti-goat IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1705
Isotype control
Goat polyclonal - 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.


Immunofluorescent analysis of HEK293 cells transfected with mCherry-HA construct (red) and stained with goat pAb to mCherry, 1536, dilution 1:2,000, in green. The blue is Hoechst staining of nuclear DNA. The 1536 antibody reveals mCherry protein expressed only in transfected cells which appear golden in color. Untransfected cells expressing no mCherry are not recognized by the antibody, as a result only their nuclei are visible.
Chromogenic immunostaining of a formalin fixed paraffin embedded section of mouse brain transduced with a TdTomato construct under an oxytocin promoter. Staining with goat pAb to mCherry, 1536, dilution 1:10,000 detected with DAB (brown) using the Vector Elite 8718C-HRP detection and reagents with citra buffer retrieval. Hematoxylin (blue) was used as the counterstain. 1536 specifically detected the soma and axons of oxytocin positive neurons in the hypothalamus. The TdTomato protein is very similar in sequence to mCherry so that our antibody strongly recognizes both proteins. Mouse select image for larger view.This antibody was made against a recombinant construct expressed in and purified from E. coli. The sequence is identical to that found in a series of widely used expression vectors and is identical to Uniprot entry D1MPT3.1 MVSKGEEDNM AIIKEFMRFK VHMEGSVNGH EFEIEGEGEG RPYEGTQTAK 51 LKVTKGGPLP FAWDILSPQF MYGSKAYVKH PADIPDYLKL SFPEGFKWER 101 VMNFEDGGVV TVTQDSSLQD GEFIYKVKLR GTNFPSDGPV MQKKTMGWEA 151 SSERMYPEDG ALKGEIKQRL KLKDGGHYDA EVKTTYKAKK PVQLPGAYNV 201 NIKLDITSHN EDYTIVEQYE RAEGRHSTGG MDELYK
Western blot analysis of HEK293 cell lysates using goat pAb to mCherry, 1536, dilution 1:1,000, in green, and rabbit pAb to GAPDH, 574, dilution 1:5,000, in red: [1] protein 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 1536 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.


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.

15558047Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent proteinShaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, Tsien RY.Nat Biotechnol. 2004 Dec;22(12):1567-72. doi: 10.1038/nbt1037. Epub 2004 Nov 21.
11050231Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine)Heikal AA, Hess ST, Baird GS, Tsien RY, Webb WW.Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):11996-2001. doi: 10.1073/pnas.97.22.11996.
11050230The structure of the chromophore within DsRed, a red fluorescent protein from coralGross LA, Baird GS, Hoffman RC, Baldridge KK, Tsien RY.Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):11990-5. doi: 10.1073/pnas.97.22.11990.
11050229Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coralBaird GS, Zacharias DA, Tsien RY.Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):11984-9. doi: 10.1073/pnas.97.22.11984.


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