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Wählen Sie konfigurierbare Panels & Premixed-Kits - ODER - Kits für die zelluläre Signaltransduktion & MAPmates™
Konfigurieren Sie Ihre MILLIPLEX® MAP-Kits und lassen sich den Preis anzeigen.
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Kits für die zelluläre Signaltransduktion & MAPmates™
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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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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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Detect phospho-ILK (Ser246) using this Anti-phospho-ILK (Ser246) Antibody validated for use in WB & IF.
More>>Detect phospho-ILK (Ser246) using this Anti-phospho-ILK (Ser246) Antibody validated for use in WB & IF. Less<<
Anti-phospho-ILK (Ser246) Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
ILK (Integrin-Linked Kinase) is an intraceullar Ser/Thr kinase with four Ankyrin-like repeats. It is known to play pivotal roles in extracellular matrix mediated signaling. ILK is known to associate with β-Integrins in addition to many other focal adhesion associated proteins. In this context, ILK is involved cell adhesion and migration. The kinase activity appears to be reduced following integrin activation, and overexpression of p59 ILK inhibits cellular adhesion to integrin substrates. Additionally, ILK has been associated with epithelial mesechymal transition (EMT) in a TGF-β1 induced Smad dependent manner (Li, 2003). Forced expression of ILK also induced the expression of MMP-2 (matrix metalloprotease 2) and promoted cell migration and invasion (Li, 2003).
References
Product Information
Format
Affinity Purified
HS Code
3002 15 90
Control
HeLa cell lysate
Presentation
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Detect phospho-ILK (Ser246) using this Anti-phospho-ILK (Ser246) Antibody validated for use in WB & IF.
Key Applications
Western Blotting
Immunofluorescence
Application Notes
Immunofluorescence Analysis: A previous lot was used by an independent laboratory in BT549 breast cancer cells. (Dr. Shoukat Dedhar, BC Cancer Research Centre, Vancouver, BC, Canada.)
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to human ILK phosphorylated at Ser246.
Epitope
Phosphorylated Ser246
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
This antibody recognizes ILK when phosphorylated at Ser246.
Species Reactivity
Human
Mouse
Rat
Ox
Species Reactivity Note
Demonstrated to react with human, mouse, and rat. Predicted to react with ox based on 100% sequence homology.
Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK), interacts with the cytoplasmic domain of beta-1 integrin. This gene encodes a serine/threonine protein kinase with 4 ankyrin-like repeats, which associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq].
FUNCTION: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
ENZYME REGULATION: Stimulated rapidly but transiently by both cell fibronectin interactions, as well as by insulin, in a PI3-K-dependent manner, likely via the binding of PtdIns(3,4,5)P3 with a PH-like domain of ILK.
SUBUNIT STRUCTURE: Interacts with cytoplasmic domain of beta 1 subunit of integrin. Could also interacts with beta 2, beta 3 and/or beta 5 subunit of integrin. Interacts (via ANK repeats) with LIMS1 and LIMS2. Interacts with parvins and probably TGFB1I1.
TISSUE SPECIFICTY: Highly expressed in heart followed by skeletal muscle, pancreas and kidney. Weakly expressed in placenta, lung and liver.
DOMAIN: A PH-like domain is involved in phosphatidylinositol phosphate binding.
PTM: Autophosphorylated on serine residues.
SEQUENCE SIMILARITIES: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Contains 5 ANK repeats.
Contains 1 protein kinase domain.
SEQUENCE CAUTION: The sequence CAB94832.1 differs from that shown. Reason: Probable cloning artifact. Was originally thought to be distinct gene (ILK2).
Molecular Weight
~54 kDa observed
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in HeLa cell lysate.
Western Blot Analysis: 0.1 µg/mL of this antibody detected ILK in 10 µg of HeLa cell lysate.
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.
Utrophin is normally confined to the neuromuscular junction (NMJ) in adult muscle and partially compensates for the loss of dystrophin in mdx mice. We show that Akt signaling and utrophin levels were diminished in sarcospan (SSPN)-deficient muscle. By creating several transgenic and knockout mice, we demonstrate that SSPN regulates Akt signaling to control utrophin expression. SSPN determined α-dystroglycan (α-DG) glycosylation by affecting levels of the NMJ-specific glycosyltransferase Galgt2. After cardiotoxin (CTX) injury, regenerating myofibers express utrophin and Galgt2-modified α-DG around the sarcolemma. SSPN-null mice displayed delayed differentiation after CTX injury caused by loss of utrophin and Akt signaling. Treatment of SSPN-null mice with viral Akt increased utrophin and restored muscle repair after injury, revealing an important role for the SSPN-Akt-utrophin signaling axis in regeneration. SSPN improved cell surface expression of utrophin by increasing transportation of utrophin and DG from endoplasmic reticulum/Golgi membranes. Our experiments reveal functions of utrophin in regeneration and new pathways that regulate utrophin expression at the cell surface.
Sarcospan (SSPN) is a core component of the major adhesion complexes in skeletal muscle, the dystrophin- and utrophin (Utr)-glycoprotein complexes (DGC and UGC). We performed a rigorous analysis of SSPN-null mice and discovered that loss of SSPN decreased DGC and UGC abundance, leading to impaired laminin-binding activity and susceptibility to eccentric contraction-induced injury in skeletal muscle. We show that loss of SSPN increased levels of α7β1 integrin. To genetically test whether integrin compensates for the loss of DGC and UGC function in SSPN-nulls, we generated mice lacking both SSPN and α7 integrin (DKO, double knockout). Muscle regeneration, sarcolemma integrity and fibrosis were exacerbated in DKO mice and were remarkably similar to muscle from Duchenne muscular dystrophy (DMD) patients, suggesting that secondary loss of integrin contributes significantly to pathogenesis. Expression of the DGC and UGC, laminin binding and Akt signaling were negatively impacted in DKO muscle, resulting in severely diminished specific force properties. We demonstrate that SSPN is a necessary component of dystrophin and Utr function and that SSPN modulation of integrin signaling is required for extracellular matrix attachment and muscle force development.
