Mouse Monoclonal Anti-VLDL-Receptor (Very Low Density Lipoprotein Receptor) [Clone VLDLR/1337]
Referentie NB-36-00851-P0
Formaat : 20ug
Merk : Neo Biotech
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VLDL-Receptor (Very Low Density Lipoprotein Receptor) Antibody [VLDLR/1337]
Applications & Dilutions
Summary
VLDLR (very low density lipoprotein receptor) is a member of the LDL receptor gene family, which includes LDL receptor, LRP, megalin, VLDLR and ApoER2. The LDL receptor family is characterized by a cluster of cysteine-rich class A repeats, epidermal growth factor (EGF)-like repeats, YWTD repeats and an O-linked sugar domain. VLDLR associates with RAP (receptor associated protein) during receptor folding, and RAP facilitates the secretion of the extracellular region of VLDLR. VLDLR is thought to mediate the interaction of extracellular Reelin and cytosolic mDab1 (mammalian disabled protein), which activates a tyrosine kinase. This pathway regulates the migration of neurons along the radial glial fiber network during brain development.
Product Properties & Targets
Functions
- Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Binds also to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU (PubMed:24381170, PubMed:30873003). In the off-state of the pathway, forms homooligomers or heterooligomers with LRP8 (PubMed:30873003). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 (PubMed:30873003). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons. Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone (By similarity).
- (Microbial infection) Acts as a receptor for Semliki Forest virus.
Key References
- Mikhailenko, I., et al. 1999. J. Cell Sci. 112: 3269-3281.
PubMed Links
- https://pubmed.ncbi.nlm.nih.gov/8128315/
- https://pubmed.ncbi.nlm.nih.gov/8069294/
- https://pubmed.ncbi.nlm.nih.gov/8294473/
- https://pubmed.ncbi.nlm.nih.gov/8020981/
- https://pubmed.ncbi.nlm.nih.gov/15164053/
- https://pubmed.ncbi.nlm.nih.gov/15489334/
- https://pubmed.ncbi.nlm.nih.gov/12857919/
- https://pubmed.ncbi.nlm.nih.gov/17330141/
- https://pubmed.ncbi.nlm.nih.gov/18039658/
- https://pubmed.ncbi.nlm.nih.gov/20427281/
- https://pubmed.ncbi.nlm.nih.gov/23701949/
- https://pubmed.ncbi.nlm.nih.gov/24381170/
- https://pubmed.ncbi.nlm.nih.gov/30873003/
- https://pubmed.ncbi.nlm.nih.gov/34929721/
- https://pubmed.ncbi.nlm.nih.gov/15064754/
- https://pubmed.ncbi.nlm.nih.gov/10391209/
- https://pubmed.ncbi.nlm.nih.gov/16080122/
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