mouse anti-mCherry monoclonal antibody (5B1) 4068

$100.00 – $2,600.00

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

SKU: 4068parent Categories: antibody, epitope tag Tags: MCherry, monoclonal, mouse

Weight	1 lbs
Dimensions	9 × 5 × 2 in
host	mouse
isotype	IgG2a
clonality	monoclonal
concentration	1 mg/mL
applications	ICC/IF, IHC, WB
available sizes	1 mg, 100 µg, 25 µg

mouse anti-mCherry monoclonal antibody (5B1) 4068

antibody
Database link: mCherry X5DSL3
Tested applications WB,IHC,IHC,ICC/IF
Recommended dilutions WB: 1:2000 IF/IHC: 1:500
Immunogen Full length recombinant protein
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 monoclonal
Isotype IgG2a
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

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

No results found

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

pmid	title	authors	citation
13911999	Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea	SHIMOMURA O, JOHNSON FH, SAIGA Y.	J Cell Comp Physiol. 1962 Jun;59:223-39. doi: 10.1002/jcp.1030590302.
12693991	A colourless green fluorescent protein homologue from the non-fluorescent hydromedusa Aequorea coerulescens and its fluorescent mutants	Gurskaya 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.
11988576	Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells	Zacharias DA, Violin JD, Newton AC, Tsien RY.	Science. 2002 May 3;296(5569):913-6. doi: 10.1126/science.1068539.
9759496	The green fluorescent protein	Tsien RY.	Annu Rev Biochem. 1998;67:509-44. doi: 10.1146/annurev.biochem.67.1.509.
8703075	Crystal structure of the Aequorea victoria green fluorescent protein	Ormö 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.