PCSK9 Inhibitor, EGF-A 

PCSK9 Inhibitor, EGF-A is a PCSK9 inhibitor with LDLR degradation inhibitory activity and LDLR recycling promoting activity. PCSK9 Inhibitor, EGF-A is a synthetic peptide consisting of 42 amino acid residues, which contains the calcium-binding site of the epidermal growth factor A domain (EGF-A). PCSK9 Inhibitor, EGF-A reduces plasma LDL cholesterol levels by maintaining hepatic LDLR levels and enhancing the clearance capacity of circulating LDL. PCSK9 Inhibitor, EGF-A can be used in research related to hypercholesterolemia, premature atherosclerosis, coronary heart disease and familial hypercholesterolemia^[1].

The binding of the PCSK9 inhibitor, EGF-A, to PCSK9 is pH- and calcium ion-dependent (K_d = 300 nM at 2 mM calcium ion concentration and pH 5.2; K_d = 1.0 nM at pH 7.4)^[1].
PCSK9 Inhibitor, EGF-A blocks the interactions between PCSK9 and low-density lipoprotein receptor (IC₅₀ = 3.4 μM), as well as very-low-density lipoprotein receptor (IC₅₀ = 4.7 μM)^[1].
PCSK9 Inhibitor, EGF-A (1.5-15) inhibits the degradation of mature low-density lipoprotein receptors in HepG2 cells in a dose-dependent manner^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

4597.07

C₁₈₈H₂₉₂N₅₈O₆₅S₆

Gly-Thr-Asn-Glu-Cys-Leu-Asp-Asn-Asn-Gly-Gly-Cys-Ser-His-Val-Cys-Asn-Asp-Leu-Lys-Ile-Gly-Tyr-Glu-Cys-Leu-Cys-Pro-Asp-Gly-Phe-Gln-Leu-Val-Ala-Gln-Arg-Arg-Cys-Glu-Asp-Ile-NH2 (disulfide bridge: Cys5-Cys16, Cys12-Cys25, Cys27-Cys39)

GTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDI-NH2 (disulfide bridge: Cys5-Cys16, Cys12-Cys25, Cys27-Cys39)

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Zhang DW, Lagace TA, Garuti R, et al.. Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation. The Journal of biological chemistry. 2007 Jun 22;282(25):18602-18612.  [Content Brief]