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
.
Catalogue Number
Ordering Description
Qty/Pack
List
This item has been added to favorites.
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.
Catalogue Number
Ordering Description
Qty/Pack
List
This item has been added to favorites.
Species
Panel Type
Selected Kit
Qty
Catalogue Number
Ordering Description
Qty/Pack
List Price
96-Well Plate
Qty
Catalogue Number
Ordering Description
Qty/Pack
List Price
Add Additional Reagents (Buffer and Detection Kit is required for use with MAPmates)
Qty
Catalogue Number
Ordering Description
Qty/Pack
List Price
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.
This item has been added to favorites.
The Product Has Been Added To Your Cart
You can now customize another kit, choose a premixed kit, check out or close the ordering tool.
Anti-Integrin αVβ3 Antibody, clone 27.1 (VNR-1) detects level of Integrin αVβ3 & has been published & validated for use in IF & IP.
More>>Anti-Integrin αVβ3 Antibody, clone 27.1 (VNR-1) detects level of Integrin αVβ3 & has been published & validated for use in IF & IP. Less<<
Anti-Integrin αVβ3 Antibody, clone 27.1 (VNR-1): Malzeme Güvenlik Bilgi Formu (MSDS) veya SDS, Analiz Sertifikası (COA) ve Kalite Uygunluk Sertifikası (COQ), dosyalar, broşürler ve diğer dokümanlar.
ITAGV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The I-domain containing integrin alpha V undergoes post-translational cleavage to yield disulfide-linked heavy and light chains, that combine with multiple integrin beta chains to form different integrins. Among the known associating beta chains (beta chains 1,3,5,6, and 8; 'ITGB1', 'ITGB3', 'ITGB5', 'ITGB6', and 'ITGB8'), each can interact with extracellular matrix ligands; the alpha V beta 3 integrin, perhaps the most studied of these, is referred to as the Vitronectin receptor (VNR). In addition to adhesion, many integrins are known to facilitate signal transduction.
FUNCTION: SwissProt: P06756 # The alpha-V integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrand factor. They recognize the sequence R-G-D in a wide array of ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. SIZE: 1048 amino acids; 116038 Da SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chain linked by a disulfide bond. Alpha-V associates with either beta-1, beta-3, beta-5, beta-6 or beta-8 subunit. Interacts with HIV-1 Tat. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: SwissProt: P06756 ## Belongs to the integrin alpha chain family. & Contains 7 FG-GAP repeats.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Maintain at -20°C in undiluted aliquots for up to 12 months from date of receipt.
Dynamic regulation of receptor function is a distinguishing feature of the integrin family of adhesion molecules and makes a significant contribution to alterations in cellular adhesive properties. The best characterized example is that of the platelet receptor alpha IIb beta 3 (glycoprotein IIb-IIIa), which does not bind soluble fibrinogen on resting platelets. Following platelet activation, the alpha IIb beta 3 binds soluble fibrinogen with moderately high affinity and platelet aggregation ensues. Similar regulation of receptor function has also been directly demonstrated for alpha 5 beta 1 and alpha M beta 2, and it is likely that it is a general property of all members of the family. The altered ligand binding affinity is due to a change in the conformation of the external domain of the receptor, in response to intracellular signals that are transmitted the length of the molecule. The cytoplasmic tails of the integrins are active participants in this regulation, and they also mediate interactions with the cytoskeleton. A number of anti-integrin monoclonal antibodies have been described which induce high affinity ligand binding, and certain of these preferentially bind to the high affinity conformation of the receptor. The alteration in conformation allows better access for macromolecular ligands to the ligand binding pocket, which has been mapped (in alpha IIb beta 3) to the amino terminal globular head of the receptor. The precise mechanism by which the activating signal is transferred from within the cell to the distal external domain remains the subject of active research.
