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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48-602MAG
Buffer Detection Kit for Magnetic Beads
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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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70564
Sigma-AldrichpET GST Fusion System 42
Popular GST fusion tag in advanced pET vectors
More>>Popular GST fusion tag in advanced pET vectors Less<<
pET GST Fusion System 42 MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
pET Expression Systems and pET pET Expression Systems and pET Expression Systems plus Competent Cells provide core reagents needed for target gene cloning and expression.
Components: pET Expression Systems Components for pET Expression Systems are similar for all systems unless otherwise stated with the specific pET Expression System description. pET Expression Systems include:
• 10 µg pET vector DNA (for each indicated plasmid)
• 0.2 ml BL21 Glycerol Stock
• 0.2 ml BL21(DE3) Glycerol Stock
• 0.2 ml BL21(DE3)pLysS Glycerol Stock
• 0.2 ml Induction Control Glycerol Stock
Components: pET Expression Systems plus Competent Cells
pET Expression Systems plus Competent Cells contain all of the components of the specific pET Expression System, as well as the following additional components, unless otherwise stated with the specific pET Expression System description:
• 0.2 ml NovaBlue Competent Cells
• 0.2 ml BL21(DE3) Competent Cells
• 0.2 ml BL21(DE3)pLysS Competent Cells
• 2 × 0.2 ml SOC Medium
• 10 µl Test Plasmid
These components are sufficient for up to 10 transformations in each host.
Purification and Detection Reagents Purification and detection reagents are
available separately. For complete product descriptions and ordering information, refer
to the Protein Purification and Antibodies, Conjugates & Detection Tools chapters.
pET Expression System 42
The pET-41a-c(+) and pET-42a-c(+) vectors incorporate the schistosomal glutathione-S-transferase (GST; GST•Tag) coding sequence as a fusion partner. The GST•Tag sequence has been reported to enhance the production and in some cases the solubility of its fusion partners (Smith 1998). When expressed in a soluble, properly folded form, GST•Tag fusion proteins can be purified with immobilized
glutathione. Gentle elution is achieved with buffers containing reduced glutathione.
Quantification of soluble GST fusions is also possible by assaying the transferase
activity. The pET-41 and -42 series feature the powerful T7lac promoter, and encode the GST•Tag (220 aa) sequence, proteolytic sites, His•Tag (6 aa) sequence, and S•Tag (15 aa) sequence.
In contrast to other commercially
available GST-fusion vectors, the Xa (IleGluGlyArg, pET-42 series) and enterokinase
(AspAspAspAspLys, pET-41 series) proteolytic cleavage sites have been engineered to allow removal of 100% of the vector-encoded sequences and the generation of native
proteins with their authentic N-terminal residues. Unfused proteins can be produced by
using the Nde I cloning site. A version of pET-41 is available as a linearized vector prepared for ligation-independent cloning (LIC) of PCR products.
Another pET vector with the GST•Tag sequence is pET-49b(+). Please see the website description for more information. The His•Tag and S•Tag
sequences enable alternative protein detection and purification procedures to be performed. For example, when enhancing purity with a separate purification method, or when purifying under denaturing conditions.
Commercial use of this Product requires a commercial license from EMD Millipore Corporation. Commercial use shall include but not be limited to (1) use of the Product or its components in manufacturing; (2) use of the Product or its components to provide a service, information, or data to others in exchange for consideration; (3) use of the Product or its components (or any derivatives thereof) for therapeutic, diagnostic or prophylactic purposes (including as part of a device, chip, assay or other product); or (4) resale of the Product or its components, whether or not such Product or its components are resold for use in research. Nothing contained herein shall be deemed to represent or warrant that additional third party rights are not required for use of this Product.
Catalogue Number
70564
Brand Family
Novagen®
References
References
Smith, D.B. and Johnson, K.S. 1988. Gene67, 31.
Product Information
Components
Fusion tag
His•Tag, GST•Tag, S•Tag
Applications
Biological Information
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code
Shipped with Blue Ice or with Dry Ice
Toxicity
Standard Handling
Storage
≤ -70°C
Avoid freeze/thaw
Avoid freeze/thaw
Do not freeze
Ok to freeze
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number
GTIN
70564
0
Documentation
pET GST Fusion System 42 Certificates of Analysis
Title
Lot Number
70564
References
Reference overview
Smith, D.B. and Johnson, K.S. 1988. Gene67, 31.
Citations
Title
F. Allemand, et al. (2007) Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Research35, 3016-3031.
Rutilio A. Fratti, et al. (2007) Stringent 3Q·1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. Journal of Biological Chemistry282, 14861-14867.
Ganna Panasyuk, et al. (2006) Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at ser 17. Journal of Biological Chemistry281, 31188-31201.
