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Merck
모든 사진(1)

문서

I0783

Sigma-Aldrich

Monoclonal Anti-ILK antibody produced in mouse

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

동의어(들):

Anti-Integrin-linked protein kinase

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.44

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

65.1, monoclonal

형태

buffered aqueous solution

분자량

antigen ~59 kDa

종 반응성

rat, human, bovine, monkey, mouse, canine

농도

~2 mg/mL

기술

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)

동형

IgG2b

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... ILK(3611)
mouse ... Ilk(16202)
rat ... Ilk(170922)

관련 카테고리

일반 설명

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).

면역원

purified mouse ILK recombinant protein.

애플리케이션

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

생화학적/생리학적 작용

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.

물리적 형태

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

면책조항

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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문서 라이브러리 방문

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)
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)
Si-Yu Guan et al.
FEBS letters, 592(1), 112-121 (2017-12-14)
Focal adhesion (FA) proteins, kindlin-2 and integrin-linked kinase (ILK), regulate cell adhesion and migration. ILK interacts with and promotes kindlin-2 targeting to FAs. Leu353 and Leu357 in kindlin-2 have been reported to be important for the interaction between kindlin-2 and

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