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anti-Human Parvin alpha Antikörper:
anti-Rat (Rattus) Parvin alpha Antikörper:
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Human Polyclonal Parvin alpha Primary Antibody für WB - ABIN527638
Park, Rha, Ahn, Shin, Kwon, Kim, An, Kim, Yang, Chung: PINCH-2 presents functional copy number variation and suppresses migration of colon cancer cells by paracrine activity. in International journal of cancer. Journal international du cancer 2015
edited form of miR-378a-3p preferentially binds to the 3'-UTR of the PARVA oncogene and inhibits its expression, thus preventing the progression of melanoma towards the malignant phenotype
Protein expression of alpha-Parvin increases with colorectal cancer progression.
PARVA promotes metastasis by modulating ILK signalling pathway in lung adenocarcinoma
alpha-pv-deficient HUVECs show reduced stable adherens junctions, decreased monolayer formation, and impaired motility, associated with reduced formation of integrin-mediated cell-extracellular matrix adhesion structures and an altered actin cytoskeleton.
alpha-Parvin, a pseudopodial constituent, was found to promote migration of breast cancer cells and to be expressed exclusively by Invasive lobular carcinoma
Actopaxin plays a role in hepatocellular carcinoma progression and metastasis, by way of regulation of cell invasiveness and motility, an epithelial-mesenchymal transition process, and chemosensitivity to cytotoxic drugs.
beta2-adaptin is shown to bind to the focal adhesion protein actopaxin and localize to focal adhesions during cells spreading in an actopaxin dependent manner
alpha-parvin, beta-parvin and migfilin were expressed in tumor cells in 53%, 2%, 28% and 53% of effusions and 57%, 20%, 83% and 25% of solid lesions, respectively.
Actopaxin phosphorylation is required for matrix degradation and cell invasion via regulation of Rho GTPase signaling.
results also identify the integrin-linked kinase (ILK) and alpha-parvin proteins as a new molecular partner and target, respectively, of the Lnk adaptor.
the alpha-parvin CH2-paxillin LD1 complex has a role in focal adhesion assembly
Mammalian parvins are likely to have arisen late in evolution from gene duplication as they share a remarkably similar exon/intron organization.
inhibition of the ILK-alpha-parvin complex is sufficient, although not necessary, for promotion of apoptosis
Phosphorylation of actopaxin regulates cell spreading and migration.
the association between actopaxin and TESK1, which is likely regulated by phosphorylation of actopaxin, regulates TESK1 activity and subsequent cellular spreading on fibronectin
An unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell.
this study has identified a new role for Parvin and alphaPix downstream of the integrin-ILK signaling axis for mammary epithelial cell differentiation.
[Alpha-pv deletion in ECs in mice results in multiple vascular defects characterized by decreased vascular density due to reduced vessel sprouting and compromised vessel stability.
These results provide important evidence for a crucial role of the PINCH-1-ILK-alpha-parvin complex in the control of podocyte adhesion, morphology, and survival.
Results describe the roles of the ILK-PINCH-parvin triad proteins in the maturation of focal adhesions.
Findings show that alpha-pv represents an essential adhesion checkpoint that controls RhoA/ROCK-mediated contractility in vSMCs.
This gene encodes a member of the parvin family of actin-binding proteins. Parvins are associated with focal contacts and contain calponin homology domains that bind to actin filaments. The encoded protein is part of the integrin-linked kinase signaling complex and plays a role in cell adhesion, motility and survival.
, calponin-like integrin-linked kinase-binding protein
, matrix-remodeling-associated protein 2
, parvin, alpha