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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Integrin a5/b1 purified from smooth muscle and placental tissue under nondenaturing conditions by affinity chromatography on fibronectin-sepharose (Belkin, 1990).
Two main protein bands corresponding to a5 (145 kD) and beta1 (120 kD) subunits are seen in silver stained 7.5%
polyacrylamide gels under nonreduced conditions. Minor protein band at the 210 kD corresponding to beta1 subunit disulfide dimmer, which is formed during electrophoresis and disappears after reduction.
Alternate Names
VLA-5
References
Product Information
Presentation
Purified protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 2 mM MgCl2 containing 0.2% Triton X-100. No preservatives. Source material for the enclosed purified human proteins, Integrin alpha5beta1, has been tested for antibodies to HIV, HCV, and HbsAg and found to be negative by an approved test.
Electrophoresis and Immunoblotting control. Due to the existance of reduction sensitive sites within the integrin subunits, it is recommended that gels be run under non-reducing conditions for best results. Under non-reducing conditions, the alpha5 subunit will migrate at 155 kDa while the beta1 subunit will migrate at 110 kDa.
Function: Liposomes containing Integrin alpha5/beta1 adhere to surfaces coated with fibronectin in an RGD-dependent fashion.
Biological Information
Purity
Nonreduced SDS-PAGE of 15 μg on 5-15% polyacrylamide slab gel and staining with Coomassie shows only two main bands at 110 kDa (beta1 subunit) and 155 kDa (alpha5 subunit). A weak band at 205 kDa is due to dimerization of the b1 subunit (Belkin et al., 1996).
The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes the integrin alpha 5 chain. Alpha chain 5 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains that join with beta 1 to form a fibronectin receptor. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.
FUNCTION: SwissProt: P08648 # Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. SIZE: 1049 amino acids; 114536 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-5 associates with beta-1. Interacts with HPS5. Interacts with HIV-1 Tat. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: SwissProt: P08648 ## Belongs to the integrin alpha chain family. & Contains 7 FG-GAP repeats.
Physicochemical Information
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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 -70°C in undiluted aliquots. Avoid repeated freeze/thaw cycles.
Self-assembling multimeric integrin alpha5beta1 ligands for cell attachment and spreading. M Kreiner,Z Li,J Beattie,S M Kelly,H J Mardon,C F van der Walle Protein engineering, design & selection : PEDS
21
2008
Substrates utilising clustered arginine-glycine-aspartic acid (RGD) ligand displays support greater cell adhesion over random displays. However, cell adhesion to integrin alpha5beta1 requires the synergy site on the 9th type III fibronectin domain (FIII) in addition to RGD on the 10th FIII domain. Here, we have designed and expressed soluble protein chimeras consisting of an N-terminal 9th-10th FIII domain pair, IgG-derived hinge and leucine zipper-derived helix; the latter mutated to yield di-, tri- and tetrameric coiled coils and thus self-assembling, multimeric integrin alpha5beta1 ligands. A unique C-terminal cysteine was appended to the helix to facilitate 'anchoring' of the chimeras with a defined orientation on a surface. Size-exclusion chromatography and circular dichroism demonstrated that the chimeras self-assembled as multimers in solution with defined secondary structures predicted from theoretical calculations. Biotinylation via a thioether bond was used to selectively bind the chimeras to streptavidin-coated surfaces, each of which was then shown to bind integrin alpha5beta1 by surface plasmon resonance. Spreading of fibroblasts to surfaces derivatised with the chimeras was found to proceed in the order: tetramer > trimer > dimer > monomer. Thus, we describe novel polyvalent integrin alpha5beta1 ligands for facile derivatisation of substrates to improve cell adhesion in vitro.