Our broad portfolio consists of multiplex panels that allow you to choose, within the panel, analytes that best meet your needs. On a separate tab you can choose the premixed cytokine format or a single plex kit.
Cell Signaling Kits & MAPmates™
Choose fixed kits that allow you to explore entire pathways or processes. Or design your own kits by choosing single plex MAPmates™, following the provided guidelines.
The following MAPmates™ should not be plexed together:
-MAPmates™ that require a different assay buffer
-Phospho-specific and total MAPmate™ pairs, e.g. total GSK3β and GSK3β (Ser 9)
-PanTyr and site-specific MAPmates™, e.g. Phospho-EGF Receptor and phospho-STAT1 (Tyr701)
-More than 1 phospho-MAPmate™ for a single target (Akt, STAT3)
-GAPDH and β-Tubulin cannot be plexed with kits or MAPmates™ containing panTyr
.
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Select A Species, Panel Type, Kit or Sample Type
To begin designing your MILLIPLEX® MAP kit select a species, a panel type or kit of interest.
Custom Premix Selecting "Custom Premix" option means that all of the beads you have chosen will be premixed in manufacturing before the kit is sent to you.
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Add Additional Reagents (Buffer and Detection Kit is required for use with MAPmates)
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
Space Saver Option Customers purchasing multiple kits may choose to save storage space by eliminating the kit packaging and receiving their multiplex assay components in plastic bags for more compact storage.
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Description
Overview
Recombinant, human methylated ubiquitin. A derivative of ubiquitin in which lysine residues are reductively methylated. Methylated ubiquitin can ligate to protein substrates, but does not form polyubiquitin chains. Protein breakdown rates obtained with methylated ubiquitin are slower than those obtained with unmethylated ubiquitin. Useful for reducing the polyubiquitin chain length and for determining rates of ubiquitin conjugation.
Catalogue Number
662065
Brand Family
Calbiochem®
Synonyms
Me-Ub
References
References
Hershko, A. and Heller, H. 1991. J. Biol. Chem.266, 16376. Hershko, A. and Heller, H. 1985. Biochem. Biophys. Res. Commun.128, 1079. Jentoft, N. and Dearborn, D.G. 1983. Methods. Enz.91, 570. Jentoft, N. and Dearborn, D.G. 1980. Anal. Biochem.106, 186. Jentoft, N. and Dearborn, D.G. 1979. J. Biol. Chem.254, 4359.
Ubiquitin, Methylated, Human, Recombinant Certificates of Analysis
Title
Lot Number
662065
References
Reference overview
Hershko, A. and Heller, H. 1991. J. Biol. Chem.266, 16376. Hershko, A. and Heller, H. 1985. Biochem. Biophys. Res. Commun.128, 1079. Jentoft, N. and Dearborn, D.G. 1983. Methods. Enz.91, 570. Jentoft, N. and Dearborn, D.G. 1980. Anal. Biochem.106, 186. Jentoft, N. and Dearborn, D.G. 1979. J. Biol. Chem.254, 4359.
Data Sheet
Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.
Revision
16-September-2008 RFH
Synonyms
Me-Ub
Description
Recombinant, human methylated ubiquitin. A derivative of ubiquitin in which lysine residues are reductively methylated. Methylated ubiquitin can ligate to protein substrates, but does not form polyubiquitin chains. Protein breakdown rates obtained with methylated ubiquitin are slower than those obtained with unmethylated ubiquitin. Useful for reducing the polyubiquitin chain length and for determining rates of ubiquitin conjugation.
Form
Lyophilized solid
Recommended reaction conditions
Typical concentrations for non-rate-limiting support of in vitro conjugation reactions range from 200 µM to 1 mM depending on the reaction conditions.
Purity
≥95% by SDS-PAGE
Solubility
Aqueous buffers (50 mg/ml)
Storage
Avoid freeze/thaw -20°C
Do Not Freeze
Ok to freeze
Special Instructions
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Toxicity
Standard Handling
References
Hershko, A. and Heller, H. 1991. J. Biol. Chem.266, 16376. Hershko, A. and Heller, H. 1985. Biochem. Biophys. Res. Commun.128, 1079. Jentoft, N. and Dearborn, D.G. 1983. Methods. Enz.91, 570. Jentoft, N. and Dearborn, D.G. 1980. Anal. Biochem.106, 186. Jentoft, N. and Dearborn, D.G. 1979. J. Biol. Chem.254, 4359.
