产品名称
Anti-LRP1 (N-terminal) antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~500 kDa
species reactivity
human, mouse, rat
concentration
~1.0 mg/mL
technique(s)
indirect immunofluorescence: 2-5 μg/mL using rat NRK cells
western blot: 1-2 μg/mL using whole extract of human U87 cells
western blot: 2-4 μg/mL using whole extract of mouse C2C12 cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... LRP1(4035)
mouse ... Lrp1(16971)
rat ... Lrp1(299858)
Application
Anti-LRP1 (N-terminal) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
Biochem/physiol Actions
Anti-LRP1 (N-terminal) recognizes human, mouse, and rat LRP1 (not tested in other species).
LRP1 expression is essential for early embryonic development. LRP1 facilitates various biological processes including lipoprotein metabolism, proteinase regulation, lysosomal enzymes activation and entry of viruses and toxins into the cells. In addition, It also regulates cell signaling pathways, cell migration, and neurodevelopment. LRP1 has an ability to bind at least 30 different ligands such as lipoproteins, proteinases, proteinase-inhibitor complexes, extra cellular matrix (ECM) proteins and various intracellular proteins. It also binds to bacterial toxins and viruses.
Disclaimer
Unless otherwise stated in our catalog, our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
LDL receptor-related protein 1 (LRP1), also known as 2-macroglobulin receptor, is a large endocytic receptor, widely expressed on the surface and intracellular membranes of various cells. LRP1 is encoded by the gene mapped to human chromosome 12q13.3. The encoded protein is a member of the LDL receptor family. LRP1 is synthesized in the endoplasmic reticulum as a single-chain 600 kDa type I transmembrane glycosylated precursor that is cleaved subsequently in the Golgi complex into two subunits of 515 kDa and 85 kDa. The 515 kDa N-terminal subunit remains attached to the membrane through noncovalent association with the smaller 85 kDa C-terminal subunit, which contains the transmembrane and cytoplasmic domains.
Physical form
Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.
Preparation Note
Store at –20 °C. For continuous use, the product may be stored at 2–8 °C for up to one month. For extended storage freeze in working aliquots at –20 °C. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
常规特殊物品
此项目有
Estrogen-enhanced apical and basolateral secretion of apolipoprotein B-100 by polarized trophoblast-derived BeWo cells
Kamper M, et al.
Biochimie, 138(10), 116-123 (2017)
LRP1 Suppresses Bone Resorption in Mice by Inhibiting the RANKL-Stimulated NF-$\kappa$B and p38 Pathways During Osteoclastogenesis
Lu Di
Journal of Bone and Mineral Research, 33(10), 1773-1784 (2018)
Yang Tian et al.
Journal of cell science, 132(15) (2019-07-06)
Extracellular heat shock protein 90 alpha (eHsp90α, also known as HSP90AA1) has been widely reported to promote tumor cell motility and tumor metastasis in various types of cancer. Several extracellular proteins and membrane receptors have been identified as interacting proteins
Inflammatory mediators promote production of shed LRP1/CD91, which regulates cell signaling and cytokine expression by macrophages
Gorovoy M, et al.
Journal of Leukocyte Biology, 88(4), 769-778 (2010)
Beyond endocytosis: LRP function in cell migration, proliferation and vascular permeability
Lillis AP, et al.
Journal of Thrombosis and Haemostasis, 3(8), 1884-1893 (2005)
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