Rabbit Anti-LBR Recombinant Antibody (E398L) (CBMAB-L0769-YJ)

Name: Rabbit Anti-LBR Recombinant Antibody (E398L)
SKU: CBMAB-L0769-YJ
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

E398L

Application

ICC, IF

Specificity

Human

Antibody Isotype

IgG

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer

PBS, pH 7.4

Storage

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

Lamin B Receptor

Introduction

Lamin B receptor (LBR) belongs to the ERG4/ERG24 family. It localized in the nuclear envelope inner membrane and anchors the lamina and the heterochromatin to the membrane. LBR 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.

Entrez Gene ID

3930

UniProt ID

Q14739

Alternative Names

PHA; LMN2R; PHASK; TDRD18; DHCR14B

Function

Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:9630650, PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722).
Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity).
Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity).
Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963).

Biological Process

Cholesterol biosynthetic processManual Assertion Based On ExperimentIDA:UniProtKB
Neutrophil differentiationISS:UniProtKB
Sterol biosynthetic processManual Assertion Based On ExperimentIBA:GO_Central

Cellular Location

Nucleus inner membrane
Endoplasmic reticulum membrane
Cytoplasm
Nucleus
Nucleus; nuclear rim.

Involvement in disease

Pelger-Huet anomaly (PHA):
An autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure.
Greenberg dysplasia (GRBGD):
A rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers.
Reynolds syndrome (REYNS):
A syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis.
Pelger-Huet anomaly with mild skeletal anomalies (PHASK):
A disease characterized by abnormal nuclear shape and chromatin organization in blood granulocytes, short stature, and mild skeletal anomalies. Initial skeletal features may improve with age.

PTM

Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin.

Wesley, C. C., & Levy, D. L. (2023). Differentiation-dependent changes in lamin B1 dynamics and lamin B receptor localization. Molecular Biology of the Cell, 34(2), ar10.

Patil, S., Deshpande, S., & Sengupta, K. (2023). Nuclear envelope protein lamin B receptor protects the genome from chromosomal instability and tumorigenesis. Human Molecular Genetics, 32(5), 745-763.

Takeshima, K., Maruzuru, Y., Koyanagi, N., Kato, A., & Kawaguchi, Y. (2022). Redundant and Specific Roles of A-Type Lamins and Lamin B Receptor in Herpes Simplex Virus 1 Infection. Journal of Virology, 96(24), e01429-22.

Lämmerhirt, L., Kappelmann-Fenzl, M., Fischer, S., Pommer, M., Zimmermann, T., Kluge, V., ... & Bosserhoff, A. K. (2022). Knockdown of Lamin B1 and the corresponding lamin B receptor leads to changes in heterochromatin state and senescence induction in malignant melanoma. Cells, 11(14), 2154.

Tiago, T., Hummel, B., Morelli, F. F., Basile, V., Vinet, J., Galli, V., ... & Carra, S. (2021). Small heat-shock protein HSPB3 promotes myogenesis by regulating the lamin B receptor. Cell death & disease, 12(5), 452.

Christodoulou, A., Maimaris, G., Makrigiorgi, A., Charidemou, E., Lüchtenborg, C., Ververis, A., ... & Santama, N. (2020). TMEM147 interacts with lamin B receptor, regulates its localization and levels, and affects cholesterol homeostasis. Journal of cell science, 133(16), jcs245357.

En, A., Takauji, Y., Ayusawa, D., & Fujii, M. (2020). The role of lamin B receptor in the regulation of senescence-associated secretory phenotype (SASP). Experimental cell research, 390(1), 111927.

Castro-Obregón, S. (2020). Lamin B receptor: role on chromatin structure, cellular senescence and possibly aging. Biochemical Journal, 477(14), 2715-2720.

Arai, R., En, A., Takauji, Y., Maki, K., Miki, K., Fujii, M., & Ayusawa, D. (2019). Lamin B receptor (LBR) is involved in the induction of cellular senescence in human cells. Mechanisms of ageing and development, 178, 25-32.

Lukášová, E., Kovařík, A., & Kozubek, S. (2018). Consequences of lamin B1 and lamin B receptor downregulation in senescence. Cells, 7(2), 11.

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For research use only. Not intended for any clinical use.

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