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DYNLL1, mediated porcine circovirus type 2 intracellular trafficking.
Large dynein heads take 16-nm steps by using an overlapping hand-over-hand mechanism.
LC8 promotes assembly and stabilization of microtubules.
By yeast two-hybrid assay, the authors found that the capsid protein (CA) of bovine immunodeficiency virus interacted with the dynein light-chain component LC8.
oncogenic MYC (show MYC ELISA Kits) expression, which is synthetic lethal with Dynll1 deletion in B-2 cells, did not further reduce B-1a cell numbers in Dynll1-defcient mice. we found that the ASCIZ-DYNLL1 axis was also required for the early-juvenile development of aggressive MYC (show MYC ELISA Kits)-driven and p53 (show TP53 ELISA Kits)-deficient B cell lymphomas.
DLC-1 (show DLC1 ELISA Kits) has a positive regulatory role in endothelial cell angiogenesis.
ASCIZ and its target DYNLL1 are essential for the development and expansion of MYC (show MYC ELISA Kits)-driven B cell lymphoma.
studies demonstrate that TNS1 (show TNS1 ELISA Kits) binds to DLC1 (show DLC1 ELISA Kits) and fine-tunes its RhoGAP (show ARHGAP1 ELISA Kits) activity toward RhoA (show RHOA ELISA Kits) and that the TNS1 (show TNS1 ELISA Kits)-DLC1 (show DLC1 ELISA Kits)-RhoA (show RHOA ELISA Kits) signaling axis is critical in regulating cellular functions that lead to angiogenesis
These findings uncovered the surprising functional relevance of GTP-bound Arl3 and LC8 for the unloading regulation of dynactin-bound cargo from dynein motor.
Loss of expression of only Dlc1 (show DLC1 ELISA Kits) isoform 2 may be sufficient for the development of thymic tumors and metastasis.
Several genes and biochemical activities collaborate with the inactivation of DLC1 (show DLC1 ELISA Kits) to give rise to cell transformation in MEFs, and the identified genes are relevant to human tumors with low DLC1 (show DLC1 ELISA Kits) expression.
a key role for ASCIZ in regulating the survival of developing B cells by activating DYNLL1 expression, which may then modulate Bim (show BCL2L11 ELISA Kits)-dependent apoptosis
The ASCIZ-DYNLL1 feedback loop represents a novel mechanism for auto-regulation of gene expression, where the gene product directly inhibits the transcriptional activator while bound at its own promoter.
The Dlc1 (show DLC1 ELISA Kits) deficient cells showed altered cytoskeleton structure, increased RhoA (show RHOA ELISA Kits) activity and cellular migration.
the expression levels of DLEC1 and ITGA9 were prominently decreased in lung tumor samples
DLC1 binding to nNOS (show NOS1 PLURAL_@27096@)-calmodulin (show CALM1 PLURAL_@27096@) complex does not affect the electron transport from the reductase to the oxygenase domain.
NMR-derived secondary chemical shifts and relaxation properties show that the Chica (show FAM83D ELISA Kits) LC8 binding domain is essentially disordered with a dynamically restricted segment in one linker between motifs.
DLEC1 (show DLEC1 ELISA Kits) mediates tumor-suppressive activities through NF-kappaB (show NFKB1 ELISA Kits) signaling.
Studies indicate that dynein light chain LC8 has been termed an intrinsically disordered proteins (IDPs) dimerization 'hub' protein.
DLC1 binding motif in L is involved in cytoskeleton localization and reorganization, primary transcription regulation by DLC1, and regulation of cellular DLC1 gene expression.
DLEC1 (show DLEC1 ELISA Kits) methylation was not associated with the clinicopathological variables of gastric cancer.
The dynein light intermediate chain has a Ras-like fold with insertions that distinguish it from Ras and other previously described G proteins.
DLEC1 (show DLEC1 ELISA Kits) is down-regulated in head and neck squamous cell tumors and it's promoter methylation is not associated with the clinicopathological parameters.
Authors demonstrate that the interaction between ebola virus VP35 and dynein LC8 is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis.
DLC-1 directly binds to FBF-2 outside of the RNA-binding domain and promotes FBF-2 localization and function. This result identifies a new role for DLC-1 in post-transcriptional regulation of gene expression.
DLC-1 is functioning cell nonautonomously through the same pathway as kri-1 (show KRI1 ELISA Kits) in response to ionizing radiation-induced apoptosis.
Dynein light chain 1 (DLC-1) and its partner, dynein heavy chain 1, inhibit the proliferative cell fate, in part through regulation of METT-10, a conserved putative methyltransferase.
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.
dynein, light chain, LC8-type 1
, dynein, light chain, LC8-type 1a
, cytoplasmic light-chain dynein
, dynein light chain 1, cytoplasmic
, Deleted in liver cancer 1 protein homolog
, Rho-type GTPase-activating protein 7
, START domain-containing protein 12
, rho GTPase-activating protein 7
, stAR-related lipid transfer protein 12
, deleted in liver cancer 1 protein homolog
, rho-type GTPase-activating protein 7
, rho GTPase activating protein 7
, deleted in lung and esophageal cancer 1 transcript varient 2
, deleted in lung and esophageal cancer protein 1
, 8 kDa dynein light chain
, 8kD LC
, 8kDa LC
, dynein, cytoplasmic, light chain 1
, dynein, cytoplasmic, light peptide
, protein inhibitor of neuronal nitric oxide synthase
, protein inhibitor of nitric oxide synthase
, dynein LC8
, cytoplasmic dynein light polypeptide
, dynein, cytoplasmic, light polypeptide 1
, dynein, light chain, LC8-type 1b
, dynein light chain LC8-type 1
, dynein light chain 2
, dynein, light chain, LC8-type 2