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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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
A cell-permeable diphenylpyrazolo compound that disrupts HIV accessary protein Nef dimerization (IC50 = 3 µM in HEK293T cells) and prevents Nef-mediated Src family kinase Hck activation (IC50 = 2.8 µM) without directly affecting the catalytic activity of c-Src, Hck, Lck, or Lyn. Shown to suppress HIV and SIV viral replication (IC50/strain/culture = 1 µM/SIV ΔB670/CEM-174 and <0.3 µM/HIV-1 NL4-3/CEM-T4) and infectivity, being ineffective against the replication of Nef-defective HIV-1 mutant. Molecular docking and in vitro binding studies reveal a high-affinity B9-targeting site formed at the Nef dimerization interface and a low-affinity binding site on each Nef monomer at the dimer interface periphery.
Emert-Sedlak, L.A., et al. 2013. Chem. Biol.20, 82.
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.
A cell-permeable diphenylpyrazolo compound that is shown to disrupt HIV accessary protein Nef dimerization (IC50 = 3 µM in HEK293T cells) and prevent Nef-mediated Src family kinase (SFK) Hck activation (IC50 = 2.8 µM) without directly affecting the catalytic activity of c-Src, Hck, Lck, or Lyn (IC50 >20 µM). Shown to effectively suppress HIV and SIV viral replication (IC50 <0.3 µM in 9 d HIV-1 NL4-3-infected CEM-T4 cultures; IC50 = 1 µM in 5 d SIV ΔB670-infected CEM-174 cultures) and infectivity (45% and 50% inhibition against HIV-1 NL4-3 and SIV ΔB670, respectively, following 48 h 3 µM B9 treatment in TZM-bl reporter cells) in a Nef-dependent manner, being ineffective against the replication of Nef-defective HIV-1 mutant. Molecular docking studies predict a high-affinity B9-targeting site formed at the Nef dimerization interface and a low-affinity B9-binding site on each Nef monomer at the dimer interface periphery, with Asn126 contributing to both modes of binding. Consistently, in vitro binding studies reveal two B9 KD values of 1.72 nM and 860 nM toward full-length HIV-1 Nef and a complete loss of B9 binding toward Nef N126A/L/Q mutants.
Form
Orange powder
Intert gas (Yes/No)
Packaged under inert gas
CAS number
1596216-24-8
Chemical formula
C₁₆H₁₁ClN₆O₃S
Structure formula
Purity
≥98% by HPLC
Solubility
DMSO (2.5 mg/ml)
Storage
Protect from light
+2°C to +8°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
Emert-Sedlak, L.A., et al. 2013. Chem. Biol.20, 82.
