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Merck

I0783

Sigma-Aldrich

Monoclonal Anti-ILK antibody produced in mouse

~2 mg/mL, clone 65.1, purified immunoglobulin, buffered aqueous solution

Synonym(e):

Anti-Integrin-linked protein kinase

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.44

Konjugat:
unconjugated
application:
ARR
ICC
IHC
IP
WB
Klon:
65.1, monoclonal
Speziesreaktivität:
rat, human, bovine, monkey, mouse, canine
citations:
12
Methode(n):
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 0.5-2.0 μg/mL using whole cell extract of Chinese hamster ovary cell line (CHO cells)

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

65.1, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~59 kDa

Speziesreaktivität

rat, human, bovine, monkey, mouse, canine

Konzentration

~2 mg/mL

Allgemeine Beschreibung

Monoclonal Anti-ILK (mouse IgG2b isotype) is derived from the 65.1 hybridoma produced by the fusion of mouse myeloma cells (P3X63-Ag8.653) and splenocytes from BALB/c mice immunized with purified mouse ILK recombinant protein. Integrin-linked kinase (ILK) is a ubiquitously expressed 50-59 kDa serine/threonine kinase that has three structurally well-conserved domains. A C-terminal domain contains the kinase catalytic site as well as the binding site for integrin β1 cytoplasmic domain. A N-terminal domain contains four ankyrin repeats (ANK).

Immunogen

purified mouse ILK recombinant protein.

Anwendung

Monoclonal Anti-ILK antibody produced in mouse has been used in:
  • immunostaining
  • immunoprecipitation
  • immunocytochemistry
  • immunohistochemistry
  • western blotting

Biochem./physiol. Wirkung

Integrin-linked kinase (ILK) is a serine-threonine kinase that interacts with PINCH and parvin to modulate cell adhesion, growth, differentiation, migration and invasion. This kinase binds to integrin β1, β2 and β3 domains to regulate integrin signalling. ILK functions as a receptor-proximal effector for integrin and growth factor dependent signal transduction. ILK is associated with cell cycle progression and oncogenic transformation. The kinase activity of ILK is low in non-activated cells; its activity is stimulated by cell-extracellular matrix (ECM) interactions and by certain growth factors. Negative regulation of ILK is mediated by two phosphatases: phosphatase and tensin homolog (PTEN), a tumor suppressor lipid phosphatase and ILKAP (ILK associated serine/threonine phosphatase), a protein phosphatase 2C (PP2C) protein phosphatase. In tumor cells that do not express PTEN protein, ILK is constitutively active.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Haftungsausschluss

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.

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Die Dokumentenbibliothek aufrufen

Kindlin-2 controls TGF-beta signalling and Sox9 expression to regulate chondrogenesis
Wu C, et al.
Nature Communications, 6(1), 7531-7531 (2015)
Pinch1 is required for normal development of cranial and cardiac neural crest-derived structures
Liang X, et al.
Circulation Research, 100(4), 527-535 (2007)
Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
Wu C and Dedhar S
The Journal of Cell Biology, 155(4), 505-510 (2001)
Promoter characterization and genomic organization of the gene encoding integrin-linked kinase 1
Melchior C, et al.
Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression, 1575(1-3), 117-122 (2002)
Requirement for integrin-linked kinase in neural crest migration and differentiation and outflow tract morphogenesis
Dai X, et al.
BMC Biology, 11(1), 107-107 (2013)

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