ICC/IF image rabbit anti mCherry polyclonal antibody 2999

rabbit anti-mCherry polyclonal antibody 2999

$100.00 – $2,600.00

Antibody summary

Rabbit polyclonal to mCherry
Suitable for: WB, ICC/IF, IHC
Reacts with: tagged fusion proteins
Isotype: IgG
100 µg, 25 µg, 1 mg

SKU: 2999parent Categories: antibody, epitope tag Tags: polyclonal, rabbit

Weight	1 lbs
Dimensions	9 × 5 × 2 in
host	rabbit
isotype	IgG
clonality	polyclonal
concentration	1 mg/mL
applications	ICC/IF, IHC, WB
available sizes	1 mg, 100 µg, 25 µg

rabbit anti-mCherry polyclonal antibody 2999

antibody
Database link: mCherry X5DSL3
Tested applications WB,IHC,IHC,ICC/IF
Recommended dilutions WB: 1:1000 IF/IHC: 1:500
Immunogen Full length recombinant mCherry protein expressed in and purified from E. coli
Size and concentration 25, 100, 1000µg and 1 mg/mL
Form liquid
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
Purity affinity purified
Clonality polyclonal
Isotype IgG
Compatible secondaries goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863 goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control Rabbit 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

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

Immunofluorescent analysis of HEK293 cells transfected with mCherry-HA, construct, in red, and stained with rabbit pAb to mCherry, 2999, dilution 1:1,000, in green. The blue is Hoechst staining of nuclear DNA. 2999 antibody reveals mCherry protein expressed only in transfected cells which appear golden in color. Untransfected cells do not react with the antibody, as a result only their nuclei are visible.

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 RPYEGTQTAK51 LKVTKGGPLP FAWDILSPQF MYGSKAYVKH PADIPDYLKL SFPEGFKWER101 VMNFEDGGVV TVTQDSSLQD GEFIYKVKLR GTNFPSDGPV MQKKTMGWEA151 SSERMYPEDG ALKGEIKQRL KLKDGGHYDA EVKTTYKAKK PVQLPGAYNV201 NIKLDITSHN EDYTIVEQYE RAEGRHSTGG MDELYKChromogenic immunostaining of formalin fixed paraffin embedded oxytocin-Tdtomato Cre mouse brain section with rabbit pAb to mCherry, 2999, dilution 1:5,000, detected with DAB (brown) using the Vector Elite 8718C-HRP detection and reagents with citra buffer retrieval. Hematoxylin (blue) was used as the counterstain. 2999 specifically detected the soma and axons of Cre activated neurons expressing Tdtomato. Our antibody recognizes tdTomato since it is very similar in primary sequence to mCherry. Mouse select image at left for larger view.

Western blot analysis of HEK293 cell lysates using rabbit pAb to mCherry, 2999, dilution 1:3,000, in green, and mouse mAb to GAPDH, 5157 dilution 1:2,000, in red: [1] protein standard, [2] HEK293 control cells, [3] HEK293 cells transfected with pCI-Neo-mod vector expressing two tdTomato protein domains, [4] HEK293 cells transfected with pCI-mod vector expressing one mCherry-HA protein domain, and [5] HEK293 cells transfected with pCI-Neo-mod vector expressing one GFP domain. The 2999 antibody recognizes tdTomato and mCherry proteins revealing major bands at about 60kDa and 30kDa, in green, respectfully, but does not recognize GFP. The red band at 37kDa corresponds to GAPDH protein here used as a loading control.

Publications

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.

There are 6 publications in our database for this antibody or clone. Here are the latest 5, for more click below.

pmid	title	authors	citation
37503287	Chronic striatal cholinergic interneuron excitation induces clinically-relevant dystonic behavior in mice	Gemperli K, Lu X, Chintalapati K, Rust A, Bajpai R, Suh N, Blackburn J, Gelineau-Morel R, Kruer MC, Mingbundersuk D, O'Malley J, Tochen L, Waugh J, Wu S, Feyma T, Perlmutter J, Mennerick S, McCall J, Aravamuthan BR.	bioRxiv [Preprint]. 2023 Jul 21:2023.07.19.549778. doi: 10.1101/2023.07.19.549778.
31636119	Nucleoplasmin is a limiting component in the scaling of nuclear size with cytoplasmic volume	Chen P, Tomschik M, Nelson KM, Oakey J, Gatlin JC, Levy DL.	J Cell Biol. 2019 Dec 2;218(12):4063-4078. doi: 10.1083/jcb.201902124. Epub 2019 Oct 21.
15558047	Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein	Shaner 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.
11050231	Molecular 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.
11050230	The structure of the chromophore within DsRed, a red fluorescent protein from coral	Gross 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.