Western blot / Immunoblot (WB), Frozen Sections (C), Immunoprecipitation (IP), Immunocytochemistry/Immunofluorescence (ICC/IF), Enzyme Immunoassay (E), Paraffin Sections (P), ChIP assay (ChIP), In Situ Hybridization (ISH), Flow Cytometry (F), Dot blot (Dot)
Selected product citations ‐ of R1091AP
TRITC conjugated antibody is cited in:
1. Suzuki Y, Mogami H, Ihara H, Urano T. Unique secretory dynamics of tissue plasminogen activator and its modulation by plasminogen activator inhibitor-1 in vascular endothelial cells. Blood. 2009 Jan 8;113(2):470-8. doi: 10.1182/blood-2008-03-144279. Epub 2008 Oct 15. PubMed PMID: 18922856.
Background of GFP antibody
Green fluorescence protein (GFP) is a 27 KDa protein derived from the bioluminiscent jellyfish Aquorea victoria, emiting green light (509 nm) when excited (excitation by Blue or UV light, absorption peak at 395 nm).
GFP is a useful tool in cell biology research, as its intrinsic fluorescence can be visualized in living cells. Light-stimulated GFP fluorescence is species-independent and a fluorescence has been reported from many different types of GFP-expressing hosts, including microbes, invertebrates, vertebrates and plants. No exogenous substrates and cofactors are required for the fluorescence of GFP, since GFP autocatalytically forms a fluorescent pigment from natural amino acids present in the nascent protein.
GFP fluorescence is stable under fixation conditions and suitable for a variety of applications. GFP is widely used as a reporter (tag) for gene expression, enabling researchers to visualize and localize GFP-tagged proteins within living cells without any further staining. Other applications of GFP include measurement of distance between proteins through fluorescence energy transfer (FRET) protocols.
To increase a fluorescence intensity of GFP, chromophore mutations have been created. The Enhanced GFP has a fluorescence 35 times more intense than the wt-GFP. Mutagenesis of GFP has produced also many mutants (e.g. Yellow Fluorescent Protein, Cyan Fluorescent Protein) with warying spectral properties. Antibodies raised against full-length GFP variants should also detect other variants of the protein.
Schoch KG et al. A subset of mouse tracheal epithelial basal cells generates large colonies in vitro. Am J Physiol Lung Cell Mol Physiol 286:L631-42 (2004).
Karabay A. et al Axonal growth is sensitive to the levels of katanin, a protein that severs microtubules. The Journal of Neuroscience 24:5778-5788 (2004).Gongidi V et al. SPARC-like 1 Regulates the Terminal Phase of Radial Glia-Guided Migration in the Cerebral Cortex. Neuron 41:57-69 (2004).
Fischer AC et al. Successful transgene expression with serial doses of aerosolized rAAV2 vectors in rhesus macaques. Mol Ther 8:918-26 (2003).
Wong JM et al. Subnuclear shuttling of human telomerase induced by transformation and DNA damage. Nat Cell Biol 4:731-6 (2002).
Zhang QX et al. Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action. Biochem J 345 Pt 2:181-4 (2000).
Mesaeli N et al. Calreticulin is essential for cardiac development. J Cell Biol 144:857-68 (1999).
McCabe JB & Berthiaume LG Functional roles for fatty acylated amino-terminal domains in subcellular localization. Mol Biol Cell 10:3771-86 (1999).
Jasinska R et al. Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters. Biochem J 340 ( Pt 3):677-86 (1999).
|Rabbit||HRP||A. victoria||C, E, WB||
0.1 mg / €320.00
|IgG||Acris Antibodies GmbH|
|Goat||HRP||C, E, WB||
1 mg / €320.00
|Acris Antibodies GmbH|