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07-1458

Sigma-Aldrich

Anti-ROCK-1/2 Antibody

from rabbit, purified by affinity chromatography

Synonym(s):

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

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

biological source

rabbit

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human, mouse

technique(s)

western blot: suitable

NCBI accession no.

NP_005397.1

UniProt accession no.

Q13464

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

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

General description

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.

Specificity

This antibody recognizes ROCK-1 and ROCK-2.

Immunogen

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

Application

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

Quality

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.

Target description

158 kDa

Linkage

Replaces: 04-1121

Other Notes

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

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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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