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aPKC regulates apical localization of Lgl1 and Lgl2 to restrict elongation of microridges in developing zebrafish epidermis.
New roles and interactions for Lgl2 that are crucial for both lumenogenesis and ciliogenesis and indicate that these processes are genetically separable in zebrafish.
lgl2 is necessary for hemidesmosome formation and maintenance of the tissue integrity in the developing basal epidermis
Lgl2 and E-cadherin act antagonistically to control the localisation of integrin alpha 6 during the formation of hemidesmosomes in the developing epidermis
The crystal structures of the Dlg4 GK domain in complex with two phosphor-Lgl2 peptides reveal the molecular mechanism underlying the specific and phosphorylation-dependent Dlg/Lgl complex formation.
It is correlated with lymphatic invasion and lymph node metastasis.
Loss or aberrant Lgl2 staining was useful in identifying Barrett gastric foveolar dysplasia
Hugl-2 induces MET and suppresses Snail tumorigenesis.
Hugl1 and Hugl2 play an essential role in the maintenance of breast epithelial polarity and differentiated cell morphology, as well as growth control.
There is a role of Lgl2 immunohistochemistry as an adjunct in the diagnosis of foveolar-type gastric dysplasia.
Lgl2 differentiates pancreatic intraepithelial neoplasia-3 and ductal adenocarcinoma of the pancreas from lower-grade pancreatic intraepithelial neoplasias.
binding between Lgl2 and LGN play a role in mitotic spindle organization through regulating formation of the LGN.NuMA complex; Lgl2 forms a Lgl2.Par-6.aPKC.LGN complex, which responds to mitotic signaling to establish normal cell division
The identification and functional characterization of the promoter region ( approximately 1.2kb) of the Hugl-2 gene are reported.
Retention of Lgl2 expression is critical for the epithelial phenotype;its loss might be involved in metastasis.
We propose that Lgl2 may be a potential marker to rule out gastric epithelial dysplasia and adenocarcinoma in diagnostic specimens.
Data suggest that mammalian Llgl2 is required for proper polarized invasion of trophoblasts and efficient branching morphogenesis during placental development, but, unlike its Drosophila ortholog, it does not function as a canonical tumor suppressor gene.
The lethal (2) giant larvae protein of Drosophila plays a role in asymmetric cell division, epithelial cell polarity, and cell migration. This human gene encodes a protein similar to lethal (2) giant larvae of Drosophila. In fly, the protein's ability to localize cell fate determinants is regulated by the atypical protein kinase C (aPKC). In human, this protein interacts with aPKC-containing complexes and is cortically localized in mitotic cells. Alternative splicing results in multiple transcript variants encoding different isoforms.
lethal giant larvae 2
, lethal giant larva 2
, lethal(2) giant larvae protein homolog 2
, protein penner
, human giant larvae homolog
, lethal giant larvae-like protein 2