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Mouse Anti-LRP1 Recombinant Antibody (CBXF-2425) (CBMAB-F1864-CQ)

This product is a mouse antibody that recognizes LRP1. The antibody CBXF-2425 can be used for immunoassay techniques such as: FC, IHC-P, IF, WB.
See all LRP1 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Rabbit
Clone
CBXF-2425
Antibody Isotype
IgG1
Application
FC, IHC-P, IF, WB

Basic Information

Specificity
Human, Rabbit
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Concentration
5 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
LRP1
Entrez Gene ID
Human4035
Rabbit100338982
UniProt ID
HumanQ07954
RabbitQ9N120
Alternative Names
APR; LRP; A2MR; CD91; APOER; LRP1A; TGFBR5; IGFBP3R
Function
Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (PubMed:11907044, PubMed:12713657).
Required for early embryonic development (By similarity).
Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor (PubMed:26142438, PubMed:1702392).
Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178).
May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (PubMed:12888553).
(Microbial infection) Functions as a receptor for Pseudomonas aeruginosa exotoxin A.
Biological Process
Amyloid-beta clearanceManual Assertion Based On ExperimentTAS:BHF-UCL
Amyloid-beta clearance by cellular catabolic processManual Assertion Based On ExperimentIMP:ARUK-UCL
Amyloid-beta clearance by transcytosisManual Assertion Based On ExperimentIGI:ARUK-UCL
Aorta morphogenesisISS:BHF-UCL
Apoptotic cell clearanceISS:BHF-UCL
Astrocyte activation involved in immune responseISS:ARUK-UCL
Cellular response to amyloid-betaISS:ARUK-UCL
Enzyme linked receptor protein signaling pathwayBy SimilarityISS:BHF-UCL
Lipid metabolic processManual Assertion Based On ExperimentTAS:ARUK-UCL
Lipoprotein transport1 PublicationNAS:UniProtKB
Lysosomal transportISS:UniProtKB
Negative regulation of gene expressionBy SimilarityISS:BHF-UCL
Negative regulation of metallopeptidase activity1 PublicationIC:ARUK-UCL
Negative regulation of pathway-restricted SMAD protein phosphorylationBy SimilarityISS:BHF-UCL
Negative regulation of platelet-derived growth factor receptor-beta signaling pathwayISS:BHF-UCL
Negative regulation of SMAD protein signal transductionBy SimilarityISS:BHF-UCL
Negative regulation of smooth muscle cell migrationISS:BHF-UCL
Negative regulation of Wnt signaling pathwayISS:BHF-UCL
PhagocytosisManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of amyloid-beta clearanceISS:ARUK-UCL
Positive regulation of cell deathManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of cholesterol effluxISS:BHF-UCL
Positive regulation of endocytosisManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of lipid transportISS:BHF-UCL
Positive regulation of lysosomal protein catabolic processManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of protein bindingManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of protein localization to plasma membraneManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of transcytosisISS:ARUK-UCL
Receptor internalizationManual Assertion Based On ExperimentIDA:ComplexPortal
Receptor-mediated endocytosisManual Assertion Based On ExperimentIMP:ARUK-UCL
Regulation of actin cytoskeleton organizationISS:BHF-UCL
Regulation of cholesterol transportISS:BHF-UCL
Regulation of extracellular matrix disassemblyManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Regulation of phospholipase A2 activityISS:BHF-UCL
Retinoid metabolic processTAS:Reactome
TranscytosisManual Assertion Based On ExperimentTAS:ARUK-UCL
Transport across blood-brain barrierISS:ARUK-UCL
Cellular Location
Low-density lipoprotein receptor-related protein 1 85 kDa subunit:
Cell membrane
Membrane, coated pit
Low-density lipoprotein receptor-related protein 1 515 kDa subunit:
Cell membrane ; Peripheral membrane protein
Membrane, coated pit
Low-density lipoprotein receptor-related protein 1 intracellular domain:
Cytoplasm
Nucleus
After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.
Golgi outpost
Cytoplasm, cytoskeleton, microtubule organizing center
Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation.
Involvement in disease
Keratosis pilaris atrophicans (KPA):
A group of rare genodermatoses characterized by keratotic follicular papules, variable degrees of inflammation, and secondary atrophic scarring. Most cases are associated with an atopic diathesis and keratosis pilaris on the extensor extremities. KPA is comprised of three distinct clinical subtypes: keratosis pilaris atrophicans faciei, atrophoderma vermiculatum, and keratosis follicularis spinulosa decalvans. Affected individuals may present with features overlapping the 3 subtypes.
Topology
Extracellular: 20-4419
Helical: 4420-4444
Cytoplasmic: 4445-4544
PTM
Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane.
The N-terminus is blocked.
Phosphorylated on serine and threonine residues.
Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1.

Lee, J., Lee, H., Lee, H., Shin, M., Shin, M. G., Seo, J., ... & Park, S. (2023). ANKS1A regulates LDL receptor-related protein 1 (LRP1)-mediated cerebrovascular clearance in brain endothelial cells. Nature Communications, 14(1), 8463.

Mogensen, E. H., Poulsen, E. T., Thøgersen, I. B., Yamamoto, K., Brüel, A., & Enghild, J. J. (2022). The low-density lipoprotein receptor-related protein 1 (LRP1) interactome in the human cornea. Experimental Eye Research, 219, 109081.

Mueller, P. A., Kojima, Y., Huynh, K. T., Maldonado, R. A., Ye, J., Tavori, H., ... & Fazio, S. (2022). Macrophage LRP1 (Low-Density Lipoprotein Receptor-Related Protein 1) Is Required for the Effect of CD47 Blockade on Efferocytosis and Atherogenesis—Brief Report. Arteriosclerosis, Thrombosis, and Vascular Biology, 42(1), e1-e9.

Shi, X., Wang, Z., Ren, W., Chen, L., Xu, C., Li, M., ... & Yang, S. (2022). LDL receptor-related protein 1 (LRP1), a novel target for opening the blood-labyrinth barrier (BLB). Signal Transduction and Targeted Therapy, 7(1), 175.

Jaeschke, A., & Hui, D. Y. (2021). LDL receptor-related protein 1 and its interacting partners in tissue homeostasis. Current Opinion in Lipidology, 32(5), 301-307.

Chen, J., Su, Y., Pi, S., Hu, B., & Mao, L. (2021). The dual role of low-density lipoprotein receptor-related protein 1 in atherosclerosis. Frontiers in cardiovascular medicine, 8, 682389.

Qu, J., Fourman, S., Fitzgerald, M., Liu, M., Nair, S., Oses-Prieto, J., ... & Bhargava, A. (2021). Low-density lipoprotein receptor-related protein 1 (LRP1) is a novel receptor for apolipoprotein A4 (APOA4) in adipose tissue. Scientific reports, 11(1), 13289.

Gamboa, R., Jaramillo-Estrella, M. J., Martínez-Alvarado, M. D. R., Soto, M. E., Torres-Paz, Y. E., Gonzalo-Calvo, D. D., ... & Huesca-Gómez, C. (2021). Monocyte low-density lipoprotein receptor-related protein 1 (LRP1) expression correlates with cIMT in mexican hypertensive patients. Arquivos Brasileiros de Cardiologia, 116, 56-65.

Schöttelndreier, D., Langejürgen, A., Lindner, R., & Genth, H. (2020). Low density lipoprotein receptor-related protein-1 (LRP1) is involved in the uptake of clostridioides difficile toxin A and serves as an internalizing receptor. Frontiers in Cellular and Infection Microbiology, 10, 565465.

Benitez-Amaro, A., Pallara, C., Nasarre, L., Rivas-Urbina, A., Benitez, S., Vea, A., ... & Llorente-Cortés, V. (2019). Molecular basis for the protective effects of low-density lipoprotein receptor-related protein 1 (LRP1)-derived peptides against LDL aggregation. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1861(7), 1302-1316.

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For research use only. Not intended for any clinical use.

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