Human LRP1 Recombinant Protein

Reference:
Product nameHuman LRP1 Recombinant Protein
Uniprot IDQ07954
Uniprot linkhttp://www.uniprot.org/uniprot/Q07954
Origin speciesHomo sapiens (Human)
Expression systemProkaryotic expression
SequenceAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHLCVFSKSQQEMG
Molecular weight30.52 kDa
Protein delivered with Tag?Yes
Purity estimated40%
BufferPBS,pH 7.5 urea +8M
FormFrozen
Delivery conditionDry Ice
Delivery lead time in business days10-25
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
ApplicationsELISA,WB
Fragment TypePartial
NCBI ReferenceQ07954
Aliases /SynonymsLow Density Lipoprotein Receptor Related Protein 1, CD91, LRP, A2MR, APOER, APR, TGFBR5, Alpha-2-Macroglobulin Receptor, Prolow-density lipoprotein receptor-related protein 1, Apolipoprotein E receptor
ReferencePX-P3046
NoteFor research use only

Description of Human LRP1 Recombinant Protein

About LRP1 protein

Low density lipoprotein receptor-related protein 1 (LRP1) is a receptor located in the cell membrane of cells required in phagocytosis of apoptotic cells and endocytosis mediated by receptor. This protein is also known as alpha-2-macroglobulin receptor (A2MR), as it is involved in early embryonic development-and known as cluster of differentiation 91 (CD91), sometimes apolipoprotein E receptor (APOER). It is encoded on chromosome 12 by LRP1 gene in humans and its expression is ubiquitous. LRP1 belongs to the Low Density Lipoprotein Receptor (LDLR) family protein.

LRP1 is involved in many biological processes and signaling pathways. LRP1 protein is especially playing a key role in lipoprotein metabolism (plasma clearance of chylomicron remnants, cellular lipid homeostasis… but some functions may still be resolved to date); cell motility with kinase-dependent intracellular signaling; Amyloid Precursor Protein (APP) metabolism, and neuronal calcium signaling in neurotransmission. Some diseases such as neurodegenerative one may be caused by dysfunctions of LRP1 pathways. Indeed, LRP1 is able to link proteins from extracellular matrix, growth factor, proteases and their inhibitors.

Structure and interactions of LRP1

LRP1 is composed of two chain non-covalently linked. The α- chain, composed of four ligand-binding domain, is extracellular. These binding domains contain cysteine-rich complement-type repeats. Domains II and IV are responsible of the majority of the protein’s binding. The EGF repeats and β propeller domains allow the release of ligands in endosomes (which have lower pH conditions). The β-chain is the transmembrane domain. It contains a cytoplasmic tail composed of hundred residues. These residues compose two NPxY motifs. These motifs are responsible for the protein’s function, especially in endocytosis and signal transduction.The recombinant human LRP1 isoform is fused with a N-terminal His tag.

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