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AB167759

Recombinant mouse PCSK9 protein

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(4 Publications)

Recombinant mouse PCSK9 protein is a Mouse Full Length protein, in the 35 to 694 aa range, expressed in HEK 293 cells, with >97%, < 1 EU/µg endotoxin level, suitable for ELISA, SDS-PAGE, FuncS.

View Alternative Names

Narc1, Pcsk9, Proprotein convertase subtilisin/kexin type 9, Neural apoptosis-regulated convertase 1, Proprotein convertase 9, Subtilisin/kexin-like protease PC9, NARC-1, PC9

4 Images
Functional Studies - Recombinant mouse PCSK9 protein (AB167759)
  • FuncS

Supplier Data

Functional Studies - Recombinant mouse PCSK9 protein (AB167759)

Loaded Recombinant human LDL Receptor protein (ab220570) on Protein A Biosensor, can bind Recombinant mouse PCSK9 protein (ab167759) with an affinity constant of 2.28 nM as determined in BLI assay.

Functional Studies - Recombinant mouse PCSK9 protein (AB167759)
  • FuncS

Supplier Data

Functional Studies - Recombinant mouse PCSK9 protein (AB167759)

Immobilized Human LDL receptor protein (ab220582) at 10 μg/mL (100 μL/well) can bind ab167759 with a linear range of 0.125-1 μg/mL.

ELISA - Recombinant mouse PCSK9 protein (AB167759)
  • ELISA

Supplier Data

ELISA - Recombinant mouse PCSK9 protein (AB167759)

Immobilized Human LDL receptor protein (ab220582) at 5 μg/mL (100 μL/well) can bind Recombinant mouse PCSK9 protein (ab167759) with a linear range of 0.078-0.313 μg/mL.

SDS-PAGE - Recombinant mouse PCSK9 protein (AB167759)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant mouse PCSK9 protein (AB167759)

SDS-PAGE analysis of reduced ab167759 stained overnight with Coomassie Blue. The protein migrates as 17 kDa and 65 kDa under reducing (R) condition due to glycosylation and proteolytic digestion.

Key facts

Purity

>97% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

SDS-PAGE, ELISA, FuncS

applications

Biologically active

Yes

Biological activity

Measured by its binding ability in a functional ELISA. Immobilized Human LDL receptor protein (ab220582) at 10 μg/mL (100 μL/well) can bind ab167759 with a linear range of 0.125-1 μg/mL.

Measured by its binding ability in a BLI assay. Loaded Recombinant human LDL Receptor protein (ab220570) on Protein A Biosensor, can bind Recombinant mouse PCSK9 protein (ab167759) with an affinity constant of 2.28 nM as determined in BLI assay.

Accession

Q80W65

Animal free

No

Carrier free

No

Species

Mouse

Reconstitution

Reconstitute at 200 µg/mL in water

Storage buffer

pH: 7.4 Constituents: PBS, 5% Trehalose

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab167759 carries a polyhistidine tag at the C-terminus. This protein undergoes autocatalytic cleavage to release the pro-peptide and mature chain. The pro-peptide and mature chain are associated through non‑covalent interactions and with a calculated MW of 13.9 kDa and 58.2 kDa respectively. The protein migrates as 17 kDa and 65 kDa under reducing condition (SDS-PAGE) due to glycosylation.</p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"QDEDGDYEELMLALPSQEDGLADEAAHVATATFRRCSKEAWRLPGTYIVVLMEETQRLQIEQTAHRLQTRAARRGYVIKVLHIFYDLFPGFLVKMSSDLLGLALKLPHVEYIEEDSFVFAQSIPWNLERIIPAWHQTEEDRSPDGSSQVEVYLLDTSIQGAHREIEGRVTITDFNSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGTSLHSLRVLNCQGKGTVSGTLIGLEFIRKSQLIQPSGPLVVLLPLAGGYSRILNAACRHLARTGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGKDIIGASSDCSTCFMSQSGTSQAAAHVAGIVARMLSREPTLTLAELRQRLIHFSTKDVINMAWFPEDQQVLTPNLVATLPPSTHETGGQLLCRTVWSAHSGPTRTATATARCAPEEELLSCSSFSRSGRRRGDWIEAIGGQQVCKALNAFGGEGVYAVARCCLVPRANCSIHNTPAARAGLETHVHCHQKDHVLTGCSFHWEVEDLSVRRQPALRSRRQPGQCVGHQAASVYASCCHAPGLECKIKEHGISGPSEQVTVACEAGWTLTGCNVLPGASLTLGAYSVDNLCVARVHDTARADRTSGEATVAAAICCRSRPSAKASWVQ","proteinLength":"Full Length","predictedMolecularWeight":"72 kDa","actualMolecularWeight":null,"aminoAcidEnd":694,"aminoAcidStart":35,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"Q80W65","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Proprotein convertase subtilisin/kexin type 9 (PCSK9) is a protein responsible for the regulation of cholesterol levels by binding to low-density lipoprotein receptors (LDLR) on hepatocytes. This interaction marks the LDLRs for degradation reducing the liver's ability to clear LDL cholesterol from the blood. PCSK9 has a molecular weight of approximately 74 kDa. The protein is mainly expressed in the liver but is also found in the intestine and kidneys. PCSK9 is referred to as NARC-1 standing for neural apoptosis-regulated convertase 1 highlighting its role in the liver's cholesterol management system.
Biological function summary

PCSK9 influences cholesterol homeostasis by its important role in degrading LDL receptors. It functions independently rather than as part of larger protein complexes. PCSK9 gains particular interest in therapeutic contexts where its inhibition can lead to increased LDLR levels and enhanced clearance of LDL cholesterol. Biotinylated PCSK9 and mouse PCSK9 variants provide significant tools for experimental study. Kits such as the PCSK9 ELISA kit enable detailed measurement of PCSK9 levels in blood samples providing insights into cholesterol metabolism dynamics.

Pathways

PCSK9 operates within the lipid metabolism pathway and the cholesterol biosynthesis pathway. The protein's activity affects the fate of LDL cholesterol within these pathways. It interacts with proteins such as apolipoprotein B (ApoB) which plays a central role in the structural component of LDL particles. The modulation of these pathways by PCSK9 highlights the significance of its function in maintaining cardiovascular health and managing cholesterol levels.

PCSK9 is closely linked to hypercholesterolemia and coronary artery disease. Mutations in PCSK9 can lead to autosomal dominant hypercholesterolemia due to its effect on LDL receptor degradation. Other proteins such as ApoB and LDLR are involved in these conditions tightly interacting with PCSK9's regulatory function. A better understanding of PCSK9's role offers potential therapeutic targets for cardiovascular disease interventions especially through the development of PCSK9 antibodies and PCSK9 assays that adjust cholesterol levels.
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Specifications

Form

Lyophilized

Additional notes

ab167759 is lyophilized from 0.22 µm filtered solution.Purified by Immobilized metal affinity chromatography.

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General info

Function

Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members : low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways.

Sequence similarities

Belongs to the peptidase S8 family.

Post-translational modifications

Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation.. Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity).. Phosphorylation protects the propeptide against proteolysis.

Subcellular localisation

Endosome

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Product protocols

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Target data

Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members : low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways.
See full target information Pcsk9
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Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Nanoscale advances : PubMed39430302

2024

Experimental VLP vaccine displaying a furin antigen elicits production of autoantibodies and is well tolerated in mice.

Applications

Unspecified application

Species

Unspecified reactive species

Vili Lampinen,Markus J T Ojanen,Fernanda Muñoz Caro,Stina Gröhn,Minna M Hankaniemi,Marko Pesu,Vesa P Hytönen

Theranostics 13:2914-2929 PubMed37284459

2023

PCSK9 attenuates efferocytosis in endothelial cells and promotes vascular aging.

Applications

Unspecified application

Species

Unspecified reactive species

Shijie Liu,Jinzi Wu,Amanda Stolarz,Huiliang Zhang,Marjan Boerma,Stephanie D Byrum,Nancy J Rusch,Zufeng Ding

PloS one 13:e0191895 PubMed29438441

2018

Development of vaccine for dyslipidemia targeted to a proprotein convertase subtilisin/kexin type 9 (PCSK9) epitope in mice.

Applications

Unspecified application

Species

Unspecified reactive species

Ryo Kawakami,Yoichi Nozato,Hironori Nakagami,Yuka Ikeda,Munehisa Shimamura,Shota Yoshida,Jiao Sun,Tomohiro Kawano,Yoichi Takami,Takahisa Noma,Hiromi Rakugi,Tetsuo Minamino,Ryuichi Morishita

Journal of lipid research 59:207-223 PubMed29180444

2017

PCSK9 deficiency reduces atherosclerosis, apolipoprotein B secretion, and endothelial dysfunction.

Applications

Unspecified application

Species

Unspecified reactive species

Hua Sun,Ronald M Krauss,Jeffrey T Chang,Ba-Bie Teng
View all publications
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