Rabbit Polyclonal Lamin B Receptor/LBR antibody. Suitable for IP, ICC/IF and reacts with Human samples. Cited in 7 publications.
pH: 6 - 8.5
Preservative: 0.05% Sodium azide
Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS
IP | ICC/IF | |
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Human | Tested | Tested |
Species | Dilution info | Notes |
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Species Human | Dilution info - | Notes - |
Species | Dilution info | Notes |
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Species Human | Dilution info - | Notes - |
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Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). 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).
Delta(14)-sterol reductase LBR, Delta-14-SR, 3-beta-hydroxysterol Delta (14)-reductase, C-14 sterol reductase, Integral nuclear envelope inner membrane protein, LMN2R, Lamin-B receptor, Sterol C14-reductase, C14SR, LBR
Rabbit Polyclonal Lamin B Receptor/LBR antibody. Suitable for IP, ICC/IF and reacts with Human samples. Cited in 7 publications.
pH: 6 - 8.5
Preservative: 0.05% Sodium azide
Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS
ab122919 is affinity purified using recombinant immunogen.
The Lamin B Receptor (LBR) also known as L. B. R. L B R or lamin B is a protein located in the inner nuclear membrane. This protein has a molecular mass of approximately 70 kDa. It acts as a receptor for lamin proteins specifically lamin B. The LBR mediates the attachment of heterochromatin and lamins to the inner nuclear membrane playing a structural role in the maintenance of nuclear architecture. It is widely expressed in various tissues notably in cells involved in rapidly proliferating tissues.
The LBR protein serves several critical functions beyond its mechanical duties. It participates in the regulation of chromatin organization and gene expression owing to its interaction with chromatin-related proteins. LBR is part of the nuclear envelope lattice and forms complexes with lamin proteins and heterochromatin. This association supports its role in anchoring chromatin at the nuclear periphery modulating processes such as DNA replication and transcription.
The LBR plays pivotal roles in nuclear envelope assembly and chromatin organization. It holds significance in the cholesterol biosynthesis pathway where it metabolizes sterol intermediates to cholesterol. This function relates LBR to other proteins including lamin A/C which collaborate in maintaining nuclear shape and function. Together they orchestrate various cellular processes important for cell cycle progression and differentiation.
Alterations in LBR function have links to conditions such as Pelger-Huët anomaly and Greenberg skeletal dysplasia. Pelger-Huët anomaly manifests as a benign hematologic condition with defective nuclear shape in neutrophils while Greenberg dysplasia is characterized by skeletal abnormalities. In these contexts LBR connects to lamin B and other nuclear envelope proteins that contribute to the pathophysiological features observed in these disorders.
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Identification of Lamin B Receptor/LBR in crude extract of HeLa cells by immuno-precipitation using ab122919, followed by Western blotting.
All lanes: Immunoprecipitation - Anti-Lamin B Receptor/LBR antibody (ab122919)
Predicted band size: 71 kDa
Indirect immuno-fluorescence staining of HeLa cells using ab122919.
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