mCherry Antibody

Images

 
Western Blot: mCherry Antibody [NBP2-43727] - Non-transfected (-) and transfected (+) 293T whole cell extracts (30 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with mCherry antibody diluted at ...read more
Immunoprecipitation: mCherry Antibody [NBP2-43727] - Analysis of 293T whole cell lysate/extractA : 20 ug whole cell lysate/extract of mcherry protein expressing 293T cellsB : Control with 2.5 ug of pre-immune rabbit ...read more

Product Details

Summary
Reactivity All-NASpecies Glossary
Applications WB, ICC/IF, IP
Clonality
Polyclonal
Host
Rabbit
Conjugate
Unconjugated

Order Details

mCherry Antibody Summary

Immunogen
Recombinant protein conjugated synthetic peptide encompassing a sequence within the center region of mCherry. The exact sequence is proprietary.
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Purity
Immunogen affinity purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

Applications/Dilutions

Dilutions
  • Immunocytochemistry/Immunofluorescence
  • Immunoprecipitation 1:100-1:500
  • Western Blot 1:500-1:3000
Theoretical MW
27 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publication using NBP2-43727.

Packaging, Storage & Formulations

Storage
Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles.
Buffer
PBS, 20% Glycerol (pH7).
Preservative
0.025% Proclin 300
Purity
Immunogen affinity purified

Alternate Names for mCherry Antibody

  • DSRED
  • mCherry
  • red fluorescent protein mCherry
  • Red Fluoroscent Protein

Background

mCherry is a monomeric red fluorescent protein (mRFP) belonging to the mFruits family which is brighter and more photostable compared to the first-generation mRFP1, making them ideal for fluorescence microscopy (1). mCherry has an excitation maximum at 587 nm and an emission maximum at 610 nm. mCherry protein was derived from DsRed, a red fluorescent protein from the coral Discosoma (disc anemone) (2). The red chromophore of DsRed has a similar topology to GFP, the green fluorescent protein isolated from the jellyfish Aequorea Victoria, but has extended pi-electron conjugation resulting in red-shifted absorbance and emission (3). mCherry is 236 amino acids (aa) in length with a theoretical molecular weight of 28 kDa and has a crystal structure with the chromophore forming a central helix shielded within an eleven-stranded beta-barrel (3).

mCherry can be used as a long-wavelength hetero-FRET (fluorescence resonance energy transfer) acceptor and probe for homoFRET experiments given its high peak molar absorptivity, folding efficiency, and superior spectral properties (4). Additionally, because mCherry does not interfere with other plasmids or alter the growth of Legionella species during intracellular growth, it can be used for constitutive gene expression in a variety of gram-negative bacterial species (5). For example, a plasmid developed to constitutively express mCherry under the Ptac promoter has been used in several Legionella species including L. pneumophila, the causative agent of Legionnaires' disease (5).

References

1. Shaner, N. C., Steinbach, P. A., & Tsien, R. Y. (2005). A guide to choosing fluorescent proteins. Nature Methods, 2(12), 905-909. doi:10.1038/nmeth819

2. Bevis, B. J., & Glick, B. S. (2002). Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nature Biotechnology, 20(1), 83-87. https://doi.org/10.1038/nbt0102-83

3. Wall, M. A., Socolich, M., & Ranganathan, R. (2000). The structural basis for red fluorescence in the tetrameric GFP homolog DsRed. Nature Structural Biology, 7(12), 1133-1138. https://doi.org/10.1038/81992

4. Akrap, N., Seidel, T., & Barisas, B. G. (2010). Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. Analytical Biochemistry, 402(1), 105-106. https://doi.org/10.1016/j.ab.2010.03.026

5. Gebhardt, M. J., Jacobson, R. K., & Shuman, H. A. (2017). Seeing red; the development of pON.mCherry, a broad-host range constitutive expression plasmid for Gram-negative bacteria. Plos One, 12(3), e0173116. https://doi.org/10.1371/journal.pone.0173116

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
⚠ WARNING: This product can expose you to chemicals including mercury, which is known to the State of California to cause reproductive toxicity with developmental effects.  For more information go to www.P65Warnings.ca.gov.

Publications for mCherry Antibody (NBP2-43727)(1)

We have publications tested in 1 confirmed species: Human.


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Product General Protocols

Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.

Video Protocols

WB Video Protocol
ICC/IF Video Protocol

FAQs for mCherry Antibody (NBP2-43727). (Showing 1 - 1 of 1 FAQ).

  1. Does this antibody cross-react with GFP epitopes? As I would like to use both GFP and mCherry antibodies during histochemistry I would not like them to cross-react.
    • mCherry and GFP share just 29% sequence similarity, so this antibody is not predicted to cross-react to GFP and has never shown any ability to detect GFP in testing.

Secondary Antibodies

 

Isotype Controls

Additional mCherry Products

Array NBP2-43727

Research Areas for mCherry Antibody (NBP2-43727)

Find related products by research area.

Blogs on mCherry.

Successful Transplantation of Friedreich Ataxia Induced Pluripotent Stem Cell (iPSC)-Derived Sensory Neurons in Dorsal Root Ganglia of Adult Rodents
Jamshed Arslan, Pharm D, PhD The dorsal root ganglia (DRG) are a collection of cell bodies of sensory nerves carrying sensory information – including nociception, mechanoreception and proprioception – from periphera...  Read full blog post.

Autophagy and RAS signaling: Clinical implications
By Christina Towers, PhD The cellular recycling process known as autophagy is currently being targeted in over 60 clinical trials focused on treating different types of cancer1. To date, the only autophagy-targeted ...  Read full blog post.

Autophagic flux: Is p62 a good indicator?
By Christina Towers, PhD Is p62 a good indicator of autophagic flux? The short answer: Yes … but … SQSTM1 encodes the cargo adaptor protein, p62, which interacts with autophagic substrates and delivers them to aut...  Read full blog post.

Make each cell count: How to assess autophagy using flow cytometry
Kristy R. Howell, PhDThe cellular recycling process known as autophagy may be induced by a variety of conditions including reduced nutrient availability, serum starvation and pharmacological agents (e.g., Rapamyci...  Read full blog post.

How to visualize autophagy by microscopy
By Christina Towers, PhD Autophagy is a recycling process that relies on the formation of a unique organelle termed an autophagosome. An elegant way to monitor autophagy is through various microscopy techniques to...  Read full blog post.

Best way to quantitatively measure Autophagic Flux
By Christina Towers, PhD Autophagy is a stress-induced cellular recycling process that plays an important physiological role in many diseases. It is induced by a variety of stimuli, both intracellular and extracel...  Read full blog post.

Animal Models to Study Autophagy
By Christina Towers, PhD What is autophagy?Autophagy is the catabolic process that degrades cytoplasmic material via the lysosome. The process of macroautophagy was originally characterized in yeast, where the...  Read full blog post.

Application Focus: I see an increase in LC3, now what?
 By Christina Towers, PhD.  Autophagy is highly conserved and tightly regulated process that all cell types use to recycle nutrients, particularly in the instance of stress1. As a result, even sm...  Read full blog post.

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