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The protein encoded by LBR belongs to the ERG4/ERG24 family. Additionally we are shipping Lamin B Receptor Antibodies (78) and many more products for this protein.
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dLBR is not a limiting component of the nuclear architecture in Drosophila cells during the first 2 days of development
Data indicate that the LBR of zebrafish and mammals are both required for correct development of embryos.
LBR targets the membrane precursor vesicles to chromatin by interacting with importin beta (show KPNB1 Proteins) in a LBR phosphorylation-dependent manner during the NE assembly at the end of mitosis
The authors demonstrate that human LBR is essential for cholesterol synthesis.
These observations point to a new mechanism regulating the localization of LBR, which is governed by an ELYS-mediated phosphorylation network.
The primary response of cells to various stresses leading to senescence consists of the down-regulation of LBR and LB1 (show CKAP2 Proteins) to attain reversal of the chromatin architecture.
We have shown here that lamin B receptor (LBR) showed a change in localization in both BrdU-induced and replicative senescent cells.
Data indicate that proto-oncogene (show RAB1A Proteins) protein c (show PROC Proteins)-akt (Akt (show AKT1 Proteins)) phosphorylates distinct sites than SRPK1 (show SRPK1 Proteins) protein within the arginine-serine (RS) domain of Lamin B Receptor (LBR).
Lamin B receptor mRNA expression was directly associated with tumor grade in breast cancer patients(grade 1 vs. grade 3 - 0.00 vs. 0.00; p = 0.0479) and Nottingham Prognostic Index (NPI1 (show KPNA1 Proteins) vs. NPI3 - 0.00 vs. 0.00; p = 0.0551).
Mutation in LBR gene is associated with pelger-huet anomaly and a mild skeletal phenotype.
Lymphohematopoietic licence: sterol C-14 reductase activity of lamin B receptor (Lbr) is essential for neutrophil differentiation.
LBR missense mutations can abolish sterol reductase activity, causing lethal Greenberg dysplasia but not Pelger anomaly
The LBR knockdown cells retain an ovoid shaped nucleus with reduced levels of lamin A/C (show LMNA Proteins) during in vitro granulopoiesis induced with retinoic acid.
The diffusional mobility of full-length LBR shows significant regional variation along the nuclear envelope, consistent with the existence of discrete LBR microdomains and the occurrence of multiple, asymmetrically-spaced anastomoses along the nuclear envelope-endoplasmic reticulum interface. Native LBR may be "configured" by long-range interactions between adjacent transmembrane domains and parts of the NH2 region.
These results show a moderate skin differentiation phenotype, which indicates that upregulation of LBR is not the sole contributor to the Hutchinson-Gilford progeria syndrome phenotype.
The N-terminal portion of LBR is probably responsible for the binding to HP1b (show CBX1 Proteins).
Study identified LBR- and lamin-A/C (show LMNA Proteins)-dependent mechanisms tethering heterochromatin to the nuclear envelope. The two tethers are sequentially used during cellular differentiation and development: first the LBR- and then the lamin-A/C (show LMNA Proteins)-dependent tether.
LBR deficiency affects not only nuclear architecture but also proliferation, cell viability, and gene expression of hematopoietic cells
sterol Delta(14) reductase domain of LBR plays a critical role in cholesterol biosynthesis and that this process is essential to both myeloid cell growth and functional maturation.
Lbr, under transcriptional regulation of C/EBPepsilon (show CEBPE Proteins), is necessary for morphological but not necessarily functional granulocyte maturation.
lamin B receptor, although residing in nuclear membranes, may contribute to cholesterol biosynthesis in Tm7sf2 (show TM7SF2 Proteins)((-/-)) mice
The protein encoded by this gene belongs to the ERG4/ERG24 family. It localized in the nuclear envelope inner membrane and anchors the lamina and the heterochromatin to the membrane. It may mediate interaction between chromatin and lamin B. Mutations of this gene has been associated with autosomal recessive HEM/Greenberg skeletal dysplasia. Alternative splicing occurs at this locus and two transcript variants encoding the same protein have been identified.
, lamin B receptor
, lamin-B receptor
, lamin-B receptor-like
, integral nuclear envelope inner membrane protein
, tudor domain containing 18
, Lamin-B receptor