Overview

Product Description	Rabbit Polyclonal antibody recognizes ApoER2
Tested Reactivity	Hu, Ms, Rat
Tested Application	IP, WB
Host	Rabbit
Clonality	Polyclonal
Isotype	IgG
Target Name	ApoER2
Antigen Species	Human
Immunogen	Synthetic peptide of Human ApoER2.
Conjugation	Un-conjugated
Alternate Names	APOER2; HSZ75190; LRP-8; Apolipoprotein E receptor 2; MCI1; Low-density lipoprotein receptor-related protein 8

Application Instructions

Application Suggestion	Tested Application Dilution IP 1:50 WB 1:500 - 1:2000
Application Note	* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.
Positive Control	C6
Observed Size	~ 110 kDa

Properties

Form	Liquid
Purification	Affinity purified.
Buffer	PBS (pH 7.4), 150 mM NaCl, 0.02% Sodium azide and 50% Glycerol.
Preservative	0.02% Sodium azide
Stabilizer	50% Glycerol
Storage Instruction	For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note	For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links	GeneID: 7804 Human LRP8 Swiss-port # Q14114 Human Low-density lipoprotein receptor-related protein 8
Gene Symbol	LRP8
Gene Full Name	low density lipoprotein receptor-related protein 8, apolipoprotein e receptor
Background	This gene encodes a member of the low density lipoprotein receptor (LDLR) family. Low density lipoprotein receptors are cell surface proteins that play roles in both signal transduction and receptor-mediated endocytosis of specific ligands for lysosomal degradation. The encoded protein plays a critical role in the migration of neurons during development by mediating Reelin signaling, and also functions as a receptor for the cholesterol transport protein apolipoprotein E. Expression of this gene may be a marker for major depressive disorder. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jun 2011]
Function	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. [UniProt]
Cellular Localization	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. [UniProt]
Calculated MW	106 kDa
PTM	O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain (By similarity). Undergoes sequential, furin and gamma-secretase dependent, proteolytic processing, resulting in the extracellular release of the entire ligand-binding domain as a soluble polypeptide and in the intracellular domain (ICD) release into the cytoplasm. The gamma-secretase-dependent proteolytical processing occurs after the bulk of the extracellular domain has been shed, in a furin-dependent manner, in alternatively spliced isoforms carrying the furin cleavage site. Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased extracellular cleavage, which in turn results in accelerating release of the intracellular domain (ICD) by the gamma-secretase. The resulting receptor fragment is able to inhibit Reelin signaling and in particular the Reelin-induced DAB1 phosphorylation (By similarity). Tyrosine phosphorylated upon apoE binding. Ubiquitinated by MYLIP leading to degradation. [UniProt]

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