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Merck
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Documenti fondamentali

07-1458

Sigma-Aldrich

Anti-ROCK-1/2 Antibody

from rabbit, purified by affinity chromatography

Sinonimo/i:

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

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

Origine biologica

rabbit

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Purificato mediante

affinity chromatography

Reattività contro le specie

human, mouse

tecniche

western blot: suitable

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

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

Descrizione generale

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.

Specificità

This antibody recognizes ROCK-1 and ROCK-2.

Immunogeno

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

Applicazioni

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

Qualità

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.

Descrizione del bersaglio

158 kDa

Linkage

Replaces: 04-1121

Altre note

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

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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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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
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
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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