Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
Apolipoprotein E Receptor 2 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q14114 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 126 KDa |
| Antigen Region | 441 - 500 aa |
| Gene ID | 7804 |
|---|---|
| Other Names | Low-density lipoprotein receptor-related protein 8, LRP-8, Apolipoprotein E receptor 2, LRP8, APOER2 |
| Target/Specificity | KLH conjugated synthetic peptide derived from human Apolipoprotein E Receptor 2 |
| Dilution | WB~~1:500 |
| Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | LRP8 |
|---|---|
| Synonyms | APOER2 |
| Function | Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands (PubMed:20223215). LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid- derived suppressor cells (By similarity). |
| Cellular Location | Cell membrane; Single-pass type I membrane protein. Secreted. Note=Isoforms that contain the exon coding for a furin- type cleavage site are proteolytically processed, leading to a secreted receptor fragment. |
| Tissue Location | Expressed mainly in brain and placenta. Also expressed in platelets and megakaryocytic cells. Not expressed in the liver. |
Provided below are standard protocols that you may find useful for product applications.
Background
Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor.
References
Kim D.-H.,et al.J. Biol. Chem. 271:8373-8380(1996).
Kim D.-H.,et al.J. Biol. Chem. 272:8498-8504(1997).
Korschineck I.,et al.J. Biol. Chem. 276:13192-13197(2001).
Gregory S.G.,et al.Nature 441:315-321(2006).
Clatworthy A.E.,et al.Neuroscience 90:903-911(1999).
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
