PCSK9 (aa 31-692) Specific Recomb™ Antibody (V3S-0224-CJ12), Human IgG2, κ (CAT#: V3S-0224-CJ12)

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Datasheet

MSDS

COA

Summary
Property
Applications
Protocols
Target
Virus Background

Summary

Description This anti-PCSK9 antibody (hF3-9) reacts with human and monkey PCSK9 proteins. It does not recognize mouse PCSK9. The parental murine monoclonal antibody (mF3-9) was generated in BALB/c mice by immunization with recombinant human PCSK9 (aa 31-692) with His tag. Anti-PCSK9 antibody can effectively antagonize the inhibition of LDL uptake by PCSK9, but cannot block the combination between PCSK9 and its ligand LDL-R.
Clonality Monoclonal
Host Species Human
Target Species Human, Monkey
Immunogen Recombinant human PCSK9 (aa 31-692) with His tag
Epitope PCSK9 ECD, aa 31-692
Affinity KD = 0.42 nM (Human PCSK9); KD = 1.27 nM (Monkey PCSK9)
Isotype Chimeric (mouse/human) IgG2, κ

Property

Expression Species HEK293F or CHO
Conjugation None
Purity >95%, determined by SDS-PAGE and SEC-HPLC
Endotoxin <1 EU/mg
Purification Protein A affinity purified
Sterility 0.2 μM filtered
Formulation PBS, pH 7.4
Preservation No preservatives
Stabilizer No stabilizers
Storage Store at 4°C within a week. For longer storage, aliquot and store at -20°C.

Applications

Application ELISA; Inhib
Application Notes The binding specificity of antibody hF3-9 to human, monkey and mouse PCSK9 was measured by ELISA.

Protocols

ELISA Enzyme-Linked Immunosorbent Assay Protocol
WB Western Blot Protocol
FC Flow Cytometry Protocol

Target

Target PCSK9
Alternative Name FH3; FHCL3; HCHOLA3; LDLCQ1; NARC-1; NARC1; PC9
Gene ID 255738
UniProt Q8NBP7
Related pathway Plasma lipoprotein assembly, remodeling, and clearance; Cholesterol metabolism
Research Area Signal Pathway; Cardiovascular
Related Disease Familial Hypercholesterolemia

Virus Background

Post Translational Modification 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.
For research use only, not directly for clinical use.
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