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07-1458

Sigma-Aldrich

Anti-ROCK-1/2 Antibody

from rabbit, purified by affinity chromatography

Sinónimos:

Renal carcinoma antigen NY-REN-35, Rho kinase, Rho-associated, coiled-coil containing protein kinase 1, Rho-associated, coiled-coil-containing protein kinase 1, p160 ROCK-1

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

origen biológico

rabbit

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

purificado por

affinity chromatography

reactividad de especies

human, mouse

técnicas

western blot: suitable

Nº de acceso NCBI

NP_005397.1

Nº de acceso UniProt

Q13464

Condiciones de envío

wet ice

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... ROCK1(6093)
mouse ... Rock1(19877)

Descripción general

Rho-Associated Kinase (Rho-Kinase or ROK) has been classified into two isoforms: ROKα/ROCK-II and ROKβ/ROCK-I. These large cellular proteins (150-160 kDa), have been reported to be involved in the formation of stress fibers, focal adhesions and cardiac hypertonic responses. Current research suggests that ROK of smooth muscle may be involved in the contractile process via phosphorylation of MYPT1 and Myosin. The serine-threonine kinase ROCK-1 is a down-stream effector of Rho, and is involved in signal transduction pathways that regulate cell morphology, motility, and tumor progression through the reorganization of the actin cytoskeleton.

Especificidad

This antibody recognizes ROCK-1 and ROCK-2.

Inmunógeno

Synthetic peptide corresponding to human ROCK-1, 90.5% homology with ROCK-2

Aplicación

This Anti-ROCK-1/2 Antibody is validated for use in WB for the detection of ROCK-1/2.

Calidad

Evaluated by Western Blot in A431 cell lysate.
Western Blot Analysis: 1:500 dilution of this antibody detected ROCK-1/2 on 10 µg of A431 cell lysate.

Descripción de destino

158 kDa

Ligadura / enlace

Replaces: 04-1121

Otras notas

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Xiang Li et al.
Oncology letters, 23(4), 129-129 (2022-03-08)
Recent studies have shown that the Eph receptor A2 (EphA2) and its inhibitor ALW-II-41-27 could regulate various cellular processes in several types of cancer. However, the manner in which ALW-II-41-27 affects the development of cervical cancer (CC) remains unknown. The
Goro Kato
eNeuro, 6(2) (2019-04-10)
Src is highly expressed in CNS neurons and contributes not only to developmental proliferation and differentiation but also to high-order brain functions, such as those contributing to alcohol consumption. Src knock-out mice exhibit no CNS abnormalities, presumably due to compensation
Mathieu Unbekandt et al.
Cell communication and signaling : CCS, 12, 54-54 (2014-10-08)
The myotonic dystrophy kinase-related CDC42-binding kinases MRCKα and MRCKβ regulate actin-myosin contractility and have been implicated in cancer metastasis. Along with the related ROCK1 and ROCK2 kinases, the MRCK proteins initiate signalling events that lead to contractile force generation which
Kenji Kashiwagi et al.
Scientific reports, 7(1), 16779-16779 (2017-12-03)
Src knockout mice show no detectable abnormalities in central nervous system (CNS) post-mitotic neurons, likely reflecting functional compensation by other Src family kinases. Cdk1- or Cdk5-dependent Ser75 phosphorylation in the amino-terminal Unique domain of Src, which shares no homology with
Nichole J Pedowitz et al.
Nature chemical biology, 17(2), 169-177 (2020-09-16)
Many intracellular proteins are modified by N-acetylglucosamine, a post-translational modification termed O-GlcNAc. This modification is found on serine and threonine side chains and has the potential to regulate signaling pathways through interplay with phosphorylation. Here, we discover and characterize one
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