Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Targets myosin phosphatase to the actin cytoskeleton. Additionally we are shipping and many more products for this protein.
Showing 10 out of 101 products:
Human Polyclonal MPRIP Primary Antibody for IF (p), IHC (p) - ABIN872987
Seifert, Werba, Tiwari, Giao Ly, Alothman, Alqunaibit, Avanzi, Barilla, Daley, Greco, Torres-Hernandez, Pergamo, Ochi, Zambirinis, Pansari, Rendon, Tippens, Hundeyin, Mani, Hajdu, Engle, Miller: The necrosome promotes pancreatic oncogenesis via CXCL1 and Mincle-induced immune suppression. in Nature 2016
Human Polyclonal MPRIP Primary Antibody for ICC, IF - ABIN4335376
Bracken, Li, Wright, Lawrence, Pillman, Salmanidis, Anderson, Dredge, Gregory, Tsykin, Neilsen, Thomson, Bert, Leerberg, Yap, Jensen, Khew-Goodall, Goodall: Genome-wide identification of miR-200 targets reveals a regulatory network controlling cell invasion. in The EMBO journal 2014
The B-Raf (show SNRPE Antibodies)(V600E) inhibitor dabrafenib selectively inhibits RIP3 (show RIPK3 Antibodies) and alleviates acetaminophen-induced liver injury.
Our data identify M-RIP as a crucial local regulator of the Rho-Rac (show AKT1 Antibodies) balance during chemotaxis and antigen recognition.
MLCP (myosin light chain phosphatase) activation is counteracted by a previously unrecognized association between MRIP and the inducible kinase NUAK2 (show NUAK2 Antibodies)
p116Rip is an important regulatory component that controls the RhoA signaling pathway, thus regulating MLCP activity and myosin phosphorylation in cells
M-RIP-dependent targeting of myosin phosphatase to stress fibers has an important role in regulating myosin light chain phosphorylation state and morphology in human vascular smooth muscle cells
A functional analysis of JNK1 (show MAPK8 Antibodies) and M-RIP with RNA interference reveals a critical role for this cascade in the invasive behavior of cancer cells.
RIP3 deletion suppresses inflammation response.
Results suggest that RGC-5 cell necroptosis following oxygen glucose deprivation is mediated by a RIP3-induced increase in oxidative stress
Lymphocyte infiltrations in the adipocyte tissue and in skin lesions of ApoE (show APOE Antibodies) single-knockout mice were significantly mitigated in ApoE (show APOE Antibodies)/RIP3 double-knockout mice
RIP3-dependent necroptosis modulates post-ischaemic adverse remodelling in a mouse model of myocardial infarction
The B-Raf (show SNRPE Antibodies)(V600E) inhibitor dabrafenib selectively inhibits RIP3 and alleviates acetaminophen-induced liver injury.
By comparing the phosphorylation sites in wild-type and RIP3-knockdown L929 cells, 174, 167, and 177 distinct phosphorylation sites were revealed to be dependent on RIP3 at the 0.5, 2, and 4 h time points after TNF (show TNF Antibodies) treatment, respectively.
p116Rip is an F-actin-binding protein (show NEXN Antibodies) with in vitro bundling activity and in vivo capability of disassembling the actomyosin-based cytoskeleton.
p116Rip oligomerizes via its C-terminal coiled-coil domain and, when overexpressed, inhibits RhoA (show RHOA Antibodies)-induced SRF activation without affecting RhoA (show RHOA Antibodies)-GTP (show AK3 Antibodies) levels.
Embryonic fibroblasts from RIP3 knockout mice are resistant to necrosis and RIP3 knockout animals are devoid of inflammation inflicted tissue damage in an acute pancreatitis model.
Using a RNA interference screen, the kinase RIP3 was identifiedas a crucial activator for programmed necrosis induced by TNF (show TNF Antibodies) and during virus infection; RIP3 regulates necrosis-specific RIP1 (show RALBP1 Antibodies) phosphorylation.
Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F- actin-binding region leads to disassembly of stress fibers in neuronal cells.
Rho interacting protein 3
, myosin phosphatase Rho-interacting protein
, Rho-interacting protein 3 (p116RIP) (RIP3)
, p116 Rho interacting protein
, myosin phosphatase-Rho interacting protein
, rho-interacting protein 3