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Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. Additionally we are shipping LCP1 Antibodies (118) and LCP1 Kits (11) and many more products for this protein.
Showing 5 out of 6 products:
Human LCP1 Protein expressed in HEK-293 Cells - ABIN2729119
Dubey, Singh, Awasthi, Nagarkoti, Kumar, Ali, Chandra, Kumar, Barthwal, Jagavelu, Sánchez-Gómez, Lamas, Dikshit: L-Plastin S-glutathionylation promotes reduced binding to β-actin and affects neutrophil functions. in Free radical biology & medicine 2015
MOLP8/R cells display a very high overexpression of LCP1 gene (l-Plastin) controlled by HIF1&alpha (show HIF1A Proteins).
these findings support a plausible mechanism by which the AP4 (show REPIN1 Proteins)/L-plastin axis is regulated by the PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins) pathway in human prostate cancer (PCa (show FLVCR1 Proteins))and may represent a novel therapeutic target in PCa (show FLVCR1 Proteins) treatment.
Mutated LCP1 is a driver of chronic lymphocytic leukemia.
AngII-dependent phosphorylation of LCP1 in cultured podocytes was mediated by the kinases ERK (show EPHB2 Proteins), p90 (show CANX Proteins) ribosomal S6 kinase (show RPS6KB1 Proteins), PKA, or PKC (show PRRT2 Proteins). LCP1 phosphorylation increased filopodia formation.
L-plastin regulates the stability of the immune synapse of naive and effector T-cells. (Review)
The findings support a mechanism in which miR (show MLXIP Proteins)-375 suppresses RUNX1 (show RUNX1 Proteins) levels, resulting in reduced vimentin (show VIM Proteins) and L-plastin expression. Knockdown of RUNX1 (show RUNX1 Proteins), L-plastin, and vimentin (show VIM Proteins) resulted in significant reductions in cell invasion in vitro, indicating the functional significance of miR (show MLXIP Proteins)-375 regulation of specific proteins involved in head and neck squamous cell carcinoma (HNSCC) invasion.
In this study, the authors found that the actin filament bundling abilities of PLS1 (show PLS1 Proteins) and PLS2 were similarly sensitive to Ca(2 (show CA2 Proteins)+) (pCa50 ~6.4), whereas PLS3 (show PLS3 Proteins) was less sensitive (pCa50 ~5.9).
elevated L-plastin expression promotes elongation and reduces protrusion density in cells with relatively lower L-plastin than fascin (show FSCN1 Proteins) levels.
Enhanced nitroxidative stress may results in LPL S-glutathionylation leading to impaired chemotaxis, polarization, and bactericidal activity of human neutrophils.
association of SNPs in LCP1 and CTIF (show KIAA0427 Proteins) with hearing
the actin-bundling protein L-plastin (LPL) is required for the perinatal development of alveolar macrophages.
Results identify L-plastin as a key effector of Mst1 (show MST1 Proteins) and establish a novel mechanism linking a signaling intermediate to an actin-binding protein (show PFN1 Proteins) critical to T cell migration.
L-plastin modulates both T- and B-cell function during the germinal center reaction and the production of T-cell-dependent antibody responses.
L-plastin may participate in signaling that enables lymphocyte transmigration
LPL-dependent actin bundling facilitates the formation of lamellipodia and normal immunological synapses and thereby enables T cell activation.
Regulation of sealing ring formation by L-plastin and cortactin (show CTTN Proteins) in osteoclasts.
We thus identify L-plastin as a molecule critical for CCR7 (show CCR7 Proteins)-mediated t-cell motility but dispensable for early CCR7 (show CCR7 Proteins) signaling.
Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. In humans, two ubiquitous plastin isoforms (L and T) have been identified. Plastin 1 (otherwise known as Fimbrin) is a third distinct plastin isoform which is specifically expressed at high levels in the small intestine. The L isoform is expressed only in hemopoietic cell lineages, while the T isoform has been found in all other normal cells of solid tissues that have replicative potential (fibroblasts, endothelial cells, epithelial cells, melanocytes, etc.). However, L-plastin has been found in many types of malignant human cells of non-hemopoietic origin suggesting that its expression is induced accompanying tumorigenesis in solid tissues.
L-plastin (Lymphocyte cytosolic protein 1) (LCP-1) (LC64P)
, Lymphocyte cytosolic protein-1 (plasmin)
, bA139H14.1 (lymphocyte cytosolic protein 1 (L-plastin))
, plastin 2
, leucocyte-specific plastin 1
, 65 kDa macrophage protein
, L-plastin (Lymphocyte cytosolic protein 1) (LCP-1) (65 kDa macrophage protein) (PP65)
, plastin 2, L
, 65 kDa matrix phosphoprotein
, Phosphoprotein UL83
, Tegument protein UL83
, involved in immune regulation
, lower matrix protein
, tegument protein pp65