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Furin convertase (R2) monoclonal antibody (MON-148)

 
ALX-803-015-R100 100 µl 323.00 USD
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Product Specification

Clone:MON-148
 
Host:Mouse
 
Isotype:IgG2a
 
Immunogen:Recombinant human furin.
 
UniProt ID:P09958
 
Source:Ascites fluid from Balb/c mice obtained after ingection of MON-148 producing hybridoma cells and isolated using a physiological salt solution (0.9% NaCl).
 
Species reactivity:Human, Mouse
 
Specificity:Recognizes epitope region 2 (R2) in the catalytic domain of furin convertase.
 
Applications:ICC, IP, WB
 
Recommended Dilutions/Conditions:Immunocytochemistry (1:200-1:400)
Immunoprecipitation (1:200; 50mM TRIS/HCl, pH 7.4, 150mM NaCl, 1% Triton X-100; 1% sodium deoxycholate, 0.1% SDS)
Western Blot (1:1,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Formulation:Liquid. Ascites fluid. Contains no preservatives.
 
Use/Stability:Stable for at least 3 months when stored at +4°C.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Blue Ice
 
Short Term Storage:+4°C
 
Long Term Storage:-20°C
 

Product Literature References

Polyphenols with indirect proprotein convertase inhibitory activity: J. Zhu, et al.; Int. J. Oncol. 43, 947 (2013), Application(s): IP, Abstract;
Generation and characterization of non-competitive furin-inhibiting nanobodies: J. Zhu, et al.; Biochem. J. 448, 73 (2012), Application(s): IP, Abstract; Full Text
A femtomol range FRET biosensor reports exceedingly low levels of cell surface furin: implications for the processing of anthrax protective antigen: K. Gawlik, et al.; PLoS One 5, e11305 (2010), Application(s): WB and ICC, Abstract; Full Text
Membrane type-1 matrix metalloprotease-independent activation of pro-matrix metalloprotease-2 by proprotein convertases: B.H. Koo, et al.; FEBS J. 276, 6271 (2009), Abstract; Full Text
Consequences of C-terminal domains and N-terminal signal peptide deletions on LEKTI secretion, stability, and subcellular distribution: A. Jayakumar, et al.; Arch. Biochem. Biophys. 435, 89 (2005), Application(s): WB and ICC, Abstract;
'Shed' furin: mapping of the cleavage determinants and identification of its C-terminus: B. Plaimauer, et al.; Biochem. J. 354, 689 (2001), Abstract;
Polyarginines are potent furin inhibitors: A. Cameron, et al.; J. Biol. Chem. 275, 36741 (2000), Abstract; Full Text
Modulation of furin-mediated proprotein processing activity by site-directed mutagenesis: J.W. Creemers, et al.; J. Biol. Chem. 268, 21826 (1993), Abstract; Full Text
Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases: W.J. Van de Ven, et al.; Crit. Rev. Oncog. 4, 115 (1993), Abstract;
Development and characterization of a panel of monoclonal antibodies against the novel subtilisin-like proprotein processing enzyme furin: H.L. van Duijnhoven, et al.; Hybridoma 11, 71 (1992), Abstract;

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