Lamin B Receptor Antibody (YA3151)
(Synonyms: PHA; LMN2R; TDRD18; DHCR14B; LBR)Based on 1 Customer Validation
Lamin B Receptor Antibody (YA3151) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Lamin B Receptor.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, FC
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Reactivity :
Human, Rat
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Formulation:
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:200-1:500 | 1:200-1:1000 |
Product Details
Lamin B Receptor Antibody (YA3151) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Lamin B Receptor.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Rat
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Observed Molecular WeightObserved band size: 58-65 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 71 kDa
A synthetic peptide of human Lamin B Receptor
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Lamin B Receptor catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis. Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation. Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation. Anchors the lamina and the heterochromatin to the inner nuclear membrane[1][2][3][4][5][6].
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Subcellular Localization
Nucleus inner membrane; Multi-pass membrane protein; Endoplasmic reticulum membrane; Cytoplasm; Nucleus
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Expression
Tissue_specificity:Expressed in the bone marrow, liver, heart, adrenal gland, lung, placenta and uterus (PubMed:16784888) . Expressed in osteoclasts and osteoblast-like cells (PubMed:21327084) -
Subunit
Interacts with CBX5 (PubMed:15882967, PubMed:9169472). Interacts with DNA (PubMed:8157662). Interaction with DNA is sequence independent with higher affinity for supercoiled and relaxed circular DNA than linear DNA (PubMed:8157662). Interacts with lamin B (PubMed:8157662). Interacts with CLNK (PubMed:26009488). Interacts with TMEM147; promoting LBR localization to the nucleus inner membrane (PubMed:32694168)
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SwissProt ID
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Synonyms
PHA; LMN2R; TDRD18; DHCR14B; LBR
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Research Field
Tags & Cell Markers
Documentation
References
[1]. Waterham HR, et al. Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene. Am J Hum Genet. 2003 Apr;72(4):1013-7. [Content Brief]
[2]. Bennati AM, et al. Sterol dependent regulation of human TM7SF2 gene expression: role of the encoded 3beta-hydroxysterol Delta14-reductase in human cholesterol biosynthesis. Biochim Biophys Acta. 2006 Jul;1761(7):677-85. [Content Brief]
[3]. Clayton P, et al. Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein. Nucleus. 2010 Jul-Aug;1(4):354-66. [Content Brief]
[4]. Tsai PL, et al. The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations. Elife. 2016 Jun 23;5:. [Content Brief]
[5]. Silve S, et al. Human lamin B receptor exhibits sterol C14-reductase activity in Saccharomyces cerevisiae. Biochim Biophys Acta. 1998 Jun 15;1392(2-3):233-44. [Content Brief]
[6]. Duband-Goulet I, et al. Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker. Biochemistry. 2000 May 30;39(21):6483-8. [Content Brief]