| Host: |
HEK293 cells |
| Reactivity: |
Human |
| Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Active Recombinant-Human PCSK9-C-His protein was developed from hek293 cells and has a target region of C-His. For use in research applications. |
| Formulation: |
Lyophilized from a 0.22 Mu m filtered solution of PBS, pH 7.4. Contact us for customized product form or formulation. |
| Immunoreactivity: |
Measured by its binding ability in a functional ELISA. Immobilized Human LDLR at 5 Mu g/mL (100 Mu L/well) can bind Human PCSK9 with a linear range of 0.5-294.7ng/mL. |
| Gene Symbol: |
PCSK9 |
| Gene ID: |
255738 |
| Uniprot ID: |
PCSK9_HUMAN |
| Immunogen Region: |
Gln31-Gln692 |
| Immunogen: |
Recombinant Human PCSK9 Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Gln31-Gln692) of human PCSK9 (Accession #NP_777596.2) fused with a 6×His tag at the C-terminus. |
| Tissue Specificity | Expressed in neuro-epithelioma, colon carcinoma, hepatic and pancreatic cell lines, and in Schwann cells. |
| 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. Phosphorylation protects the propeptide against proteolysis. |
| 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. |
| Protein Name | Proprotein Convertase Subtilisin/Kexin Type 9Neural Apoptosis-Regulated Convertase 1Narc-1Proprotein Convertase 9Pc9Subtilisin/Kexin-Like Protease Pc9 |
| Database Links | Reactome: R-HSA-381426Reactome: R-HSA-8866427Reactome: R-HSA-8957275Reactome: R-HSA-8964038 |
| Cellular Localisation | CytoplasmSecretedEndosomeLysosomeCell SurfaceEndoplasmic ReticulumGolgi ApparatusAutocatalytic Cleavage Is Required To Transport It From The Endoplasmic Reticulum To The Golgi Apparatus And For The Secretion Of The Mature ProteinLocalizes To The Endoplasmic Reticulum In The Absence Of Ldlr And Colocalizes To The Cell Surface And To The Endosomes/Lysosomes In The Presence Of LdlrThe Sorting To The Cell Surface And Endosomes Is Required In Order To Fully Promote Ldlr Degradation |
| Alternative Protein Names | Proprotein Convertase Subtilisin/Kexin Type 9 proteinNeural Apoptosis-Regulated Convertase 1 proteinNarc-1 proteinProprotein Convertase 9 proteinPc9 proteinSubtilisin/Kexin-Like Protease Pc9 proteinPCSK9 proteinNARC1 proteinPSEC0052 protein |
Information sourced from Uniprot.org
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