|The mCherry n/a (Catalog #MBS415041) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. MyBioSource\'s mCherry can be used in a range of immunoassay formats including, but not limited to, Immunofluorescence (IF), Western Blot (WB).
Try at dilutions of 1:500 and higher for immunofluorescence. For western blots try at 1:2,000. Researchers should empirically determine the suitability of the mCherry n/a for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The mCherry n/a product has the following accession number(s) (GI #410073987) (NCBI Accession #AFV60003.1). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the mCherry Antibody with the following immunoassay(s):
Western Blot (WB)
Immunogen: mCherry is an engineered derivative of one of a family of proteins originally isolated from Cnidarians (jelly fish, sea anemones and corals). The prototype for these fluorescent proteins is Green Fluorescent Protein (GFP), which is a ~27kDa protein isolated originally from the jellyfish Aequoria victoria. GFP was the basis of the 2008 Nobel Prize in Chemistry, awarded to Osamu Shimomura, Martin Chalfie and Roger Tsien, specifically "for the discovery and development of the green fluorescent protein, GFP". On expression from the GFP gene, GFP protein will fold correctly and fluoresce strongly, the development of fluoresence requires no cofactors except molecular oxygen. It can therefore be expressed in fluorescent form in essentially any prokaryotic or eukaryotic cell under aerobic conditions (1). As a result, DNA encoding GFP can be fused to DNA encoding other proteins as a means to visualize the resulting fusion protein in live cells or animals. Engineered forms of GFP and relatives have been developed to monitor Calcium levels, protease activation and a variety of other processes in real time. A whole range of GFP derivatives with different spectral properties have been developed, largely in the Tsien lab. The mCherry protein was derived from DsRed, a red fluorescent protein from so-called disc corals of the genus Discosoma. DsRed is a 223 amino acid, ~28kDa protein similar in size and properties to GFP, but, obviously, produces a red rather than a green fluorochrome. The original DsRed was engineered extensively in the Tsien lab to prevent it from forming tetramers and dimers and to modify and improve the spectral properties (2-4). The resulting monomeric protein is useful for applications such as Förster Resonance Energy Transfer (FRET, also known as Fluorescence Resonance Energy Transfer). Several further cycles of mutation, directed modification and evolutionary selection produced mCherry, which is monomeric and has an excitation maximum at 587 nm and an emission maximum at 610 nm (5). We expressed the mCherry protein sequence shown in reference 5 in bacteria, purified out the mCherry and raised several mouse monoclonal antibodies. 1C51 was affinity purified and was found to stain a band of the expected size in Hek293 cells transfected with a vector designed to express mCherry which was developed in the Tsien lab and can obtained from Clontech.