Apolipoprotein E R2/ApoE R2 Antibody - BSA Free

Western Blot: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Analysis of ApoER2 on mouse brain membrane.

Immunocytochemistry/Immunofluorescence: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Antibody was tested in Neuro-2a cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).

The identity of the AAV-BP is AAVR, the multiserotype AAV receptor. (A) Virus overlay assay of cell membrane fractions from different types of cells. Membrane proteins were extracted from various types of cells, and 100 μg of membrane proteins was used to perform a virus overlay assay with purified wild-type AAV2 particles (56). The arrow indicates a strong binding band at 150 kDa, designated AAV-BP. (B) Summary of the top five genes that correspond to the peptide sequences from the mass spectrometry analysis of the AAV-BP band. AAVR is also denoted KIAA0319L. (C) One hundred micrograms of PSA-purified HeLa S3 membrane proteins was separated on a 2-D gel and transferred onto a PVDF membrane for a virus overlay assay with rAAV2, followed by reprobing with anti-LDLR, anti-ApoER2, anti-ORP150, or anti-AAVR antibody. (D) One hundred micrograms of N- and O-deglycosylated crude HeLa S3 cell membrane proteins was separated by 2-D electrophoresis and underwent a virus overlay assay, followed by reprobing with a rabbit polyclonal antibody to integrin alpha 5. Squares indicate an identical area of the membrane. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28679762), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Knockdown of LRP8 inhibited tumor growth in vivo. (a) The pictures of nude mice injected with Lv-sh-LRP8 and corresponding control and the tumors formed after 28-day feeding. (b–c) Tumor volumes and weights were calculated between the two groups. (d) Western blotting experiments detecting the expression of Wnt/ beta -catenin signaling components and LRP8 expression in subcutaneous tumors. **p < 0.01. Three independent trials in each experiment were needed, and the data were presented as mean +/- SD. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 enhanced the metastasis of NSCLC cells. (a) Transwell analysis was performed to compare the metastasis potential in the LRP8 knockdown group. (b) H1975 cells migration and invasion capability were detected by transwell assays. The expression of proteins related to metastasis in H1299 and H460 cells (c) and H1975 cells (d) were detected by Western blotting. **p < 0.01. At least three replicate experiments were performed, and the final results were presented as mean +/- SD. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 motivated NSCLC cells development and metastasis via the Wnt/ beta -catenin signaling pathway. (a) Expression of Wnt/ beta -catenin signaling components after silencing LRP8 as detected by Western blotting assays. (b) Expression of Wnt/ beta -catenin signaling-related factors in overexpression LRP8 group of H1975 cells. CCK-8 assay (c) and colony formation analysis (d) were carried out to evaluate the proliferation abilities of H1299 and H460 cells transfected with LRP8 siRNA or negative vector or LiCl and LRP8 siRNA. (e) Invasion and migration of H1299 and H460 cells after LRP8 downregulation and LiCl addition as detected by Transwell assay. (f) Western blotting analysis for E-cadherin, Vimentin, and N-cadherin to detect the effect of LiCl in LRP8 knockdown. (g) Western blotting assays were performed to elaborate the role of LiCl in Wnt/ beta -catenin signaling-related factors induced by LRP8 silencing. **p < 0.01. Each experiment was repeated in three independent trials, and mean +/- SD was used to describe the results. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 is related to the poor prognosis of NSCLC patients. (a–c) Expression of LRP8 in NSCLC tissues as analyzed by TIMER and StarBase3.0 databases. (d) Western blotting assays to detect the expression of LRP8 in seven NSCLC cell lines and the normal bronchial epithelioid cells. (e) Immunohistochemistry staining of two representative cases showing the expression and location of LRP8 in NSCLC tissues. (f) Four-grid table showing the statistical difference of LRP8 level between tumor tissues and normal adjacent tissues. (g) Kaplan–Meier curve based on LRP8 expression in 60 NSCLC patients (log-rank test, p < 0.05). n.s, no significant difference, *p < 0.05, **p < 0.01. At least three independent biological experiments were repeated, and the data were presented as mean +/- SD. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 enhanced the metastasis of NSCLC cells. (a) Transwell analysis was performed to compare the metastasis potential in the LRP8 knockdown group. (b) H1975 cells migration and invasion capability were detected by transwell assays. The expression of proteins related to metastasis in H1299 and H460 cells (c) and H1975 cells (d) were detected by Western blotting. **p < 0.01. At least three replicate experiments were performed, and the final results were presented as mean +/- SD. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 motivated NSCLC cells development and metastasis via the Wnt/ beta -catenin signaling pathway. (a) Expression of Wnt/ beta -catenin signaling components after silencing LRP8 as detected by Western blotting assays. (b) Expression of Wnt/ beta -catenin signaling-related factors in overexpression LRP8 group of H1975 cells. CCK-8 assay (c) and colony formation analysis (d) were carried out to evaluate the proliferation abilities of H1299 and H460 cells transfected with LRP8 siRNA or negative vector or LiCl and LRP8 siRNA. (e) Invasion and migration of H1299 and H460 cells after LRP8 downregulation and LiCl addition as detected by Transwell assay. (f) Western blotting analysis for E-cadherin, Vimentin, and N-cadherin to detect the effect of LiCl in LRP8 knockdown. (g) Western blotting assays were performed to elaborate the role of LiCl in Wnt/ beta -catenin signaling-related factors induced by LRP8 silencing. **p < 0.01. Each experiment was repeated in three independent trials, and mean +/- SD was used to describe the results. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 promoted NSCLC proliferation in vitro. Western blotting experiments were conducted to validate the transfection efficiency of LRP8 siRNA in H460 and H1299 (a) and LRP8 overexpression plasmid in H1975 (d). CCK-8 assay was used to evaluate the proliferation ability of H460 and H1299 cells transfected with LRP8 siRNAs (b) and H1975 cells with LRP8 plasmid (e). (c) Colony formation analysis showing differences in H1299 and H460 cell proliferation among the three groups. (f) H1975 cell viability was measured using colony formation analysis. **p < 0.01. All experiments were performed independently at least three times, and the results were presented as mean +/- SD. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRP8 motivated NSCLC cells development and metastasis via the Wnt/ beta -catenin signaling pathway. (a) Expression of Wnt/ beta -catenin signaling components after silencing LRP8 as detected by Western blotting assays. (b) Expression of Wnt/ beta -catenin signaling-related factors in overexpression LRP8 group of H1975 cells. CCK-8 assay (c) and colony formation analysis (d) were carried out to evaluate the proliferation abilities of H1299 and H460 cells transfected with LRP8 siRNA or negative vector or LiCl and LRP8 siRNA. (e) Invasion and migration of H1299 and H460 cells after LRP8 downregulation and LiCl addition as detected by Transwell assay. (f) Western blotting analysis for E-cadherin, Vimentin, and N-cadherin to detect the effect of LiCl in LRP8 knockdown. (g) Western blotting assays were performed to elaborate the role of LiCl in Wnt/ beta -catenin signaling-related factors induced by LRP8 silencing. **p < 0.01. Each experiment was repeated in three independent trials, and mean +/- SD was used to describe the results. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35246020), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

• Reactivity: Hu, Mu, Ch, Bv
• Applications: WB, ICC/IF, PAGE
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Format: BSA Free
• Concentration: 1 mg/ml

Apolipoprotein E R2/ApoE R2 Antibody - BSA Free Summary

• Description: Novus Biologicals Rabbit Apolipoprotein E R2/ApoE R2 Antibody - BSA Free (NB100-2216) is a polyclonal antibody validated for use in WB and ICC/IF. Anti-Apolipoprotein E R2/ApoE R2 Antibody: Cited in 8 publications. All Novus Biologicals antibodies are covered by our 100% guarantee.
• Immunogen: A synthetic peptide made to a C-terminal portion of the human ApoER2 protein sequence (between residues 863-963). [UniProt# Q14114]
• Localization: Type I membrane. Isoforms that contain the exon encoding for a furin-cleavage site are proteolytically processed, leading to a secreted receptor fragment.
• Predicted Species: Bovine (95%). Backed by our 100% Guarantee.
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Gene: LRP8
• Purity: Immunogen affinity purified

Applications/Dilutions

• Dilutions:
  • Immunocytochemistry/ Immunofluorescence 1:200-1:500
  • SDS-Page reported in scientific literature (PMID 27810638)
  • Western Blot 2 ug/ml
• Application Notes: A band is seen at ~106 kDa representing the membrane form of ApoER2 in Western Blot. A larger ~130 kDa band may also be seen, representing the glycosylated form of ApoER2.

Reactivity Notes

Immunogen displays the following percentage of sequence identity for non-tested species: bovine (95%).

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS
• Preservative: 0.05% Sodium Azide
• Concentration: 1 mg/ml
• Purity: Immunogen affinity purified

Alternate Names for Apolipoprotein E R2/ApoE R2 Antibody - BSA Free

• ApoER2
• APOER2HSZ75190
• Apolipoprotein E R2
• Apolipoprotein E receptor 2
• low density lipoprotein receptor-related protein 8, apolipoprotein e receptor
• low-density lipoprotein receptor-related protein 8
• Lr8b
• LRP8
• LRP-8
• MCI1

Background

ApoER2 (apolipoprotein E receptor 2 or LDL receptor related protein 8) is a member of LDL receptor (LDLR) family and it acts as a cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. ApoER2 facilitates extracellular RELN signal transduction to intracellular signaling processes, mainly through binding with DAB1 on its cytoplasmic tail. RELN acts via both VLDLR and ApoER2 to regulate tyrosine phosphorylation mediated DAB1 activation and microtubule function in neuronal cells. ApoER2 possess higher affinity for RELN compared to VLDLR and is therefore, a key player in Reelin pathway that governs forebrain's neuronal layering during prenatal brain development. ApoER2 associates with ER resident receptor-associated protein (RAP) as well as with dimers of beta 2-glycoprotein I. In the vasculature, ApoER2 has been suggested to implicate in suppressing platelet aggregation. Moreover, ApoER2 is highly expressed in epididymis (initial segment), where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), which are required for sperm maturation. ApoER2 also function as an endocytic receptor and defective ApoER2 have been linked to myocardial infarction type 1 (MCI1).

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for Apolipoprotein E R2/ApoE R2 Antibody (NB100-2216)(8)

Publications using NB100-2216

• Tatsuaki Daimon, Atrayee Bhattacharya, Keyi Wang, Naoki Haratake, Ayako Nakashoji, Hiroki Ozawa, Yoshihiro Morimoto, Nami Yamashita, Takeo Kosaka, Mototsugu Oya, Donald W. Kufe MUC1-C is a target of salinomycin in inducing ferroptosis of cancer stem cells Cell Death Discovery 2024-01-05 [PMID: 38182558]
• Heo J, Kang H Platelet-derived growth factor-stimulated pulmonary artery smooth muscle cells regulate pulmonary artery endothelial cell dysfunction through extracellular vesicle miR-409-5p Biological chemistry 2023-10-31 [PMID: 37903646]
• Li Q, Morrill NK, Moerman-Herzog AM et al. Central repeat fragment of reelin leads to active reelin intracellular signaling and rescues cognitive deficits in a mouse model of reelin deficiency Cellular signalling 2023-06-12 [PMID: 37315752] (WB, Human)
• Fang Z, Zhong M, Zhou L et al. Low-density lipoprotein receptor-related protein 8 facilitates the proliferation and invasion of non-small cell lung cancer cells by regulating the Wnt/beta-catenin signaling pathway Bioengineered 2022-03-01 [PMID: 35246020] (WB, Human)
• Arimitsu N, Taka, K, Fujiwara N, et al. Roles of Reelin/Disabled1 pathway on functional recovery of hemiplegic mice after neural cell transplantation; Reelin promotes migration toward motor cortex and maturation to motoneurons of neural grafts Exp. Neurol. 2019-06-08 [PMID: 31185198] (ICC/IF, Mouse)
• Pillay S, Zou W, Cheng F et al. AAV serotypes have distinctive interactions with domains of the cellular receptor AAVR J. Virol. 2017-07-05 [PMID: 28679762] (WB, Human)
• Wang W, Moerman-Herzog AM, Slaton A, Barger SW Presenilin 1 mutations influence processing and trafficking of the ApoE receptor apoER2. Neurobiol. Aging 2016-10-11 [PMID: 27810638] (WB, PAGE, Mouse)
• Ding J, Bowes R C. Synaptic Expression of Apoer2 in the Plexiform Layers of Mouse Retina. J Comp Neurol 2000-07-25 [PMID: 10906706]

Bioinformatics

• Gene Symbol: LRP8