Biotin anti-human PCSK9 Antibody, PCSK9, Poly5250,BioLegend,525004

The biotinylated Poly5250 antibody is useful as the detection antibody in a sandwich ELISA assay, when used in conjunction with purified M1118E3 antibody (Cat. No. 537502) as the detection antibody and Recombinant Human PCSK9 (ELISA Std.) (Cat. No. 592509)

Host

Goat

Reactivity

Human

Application

ELISA Detection -Quality tested

Platform ID

BAB811812196

BioLegend

Headquarters

8999 BioLegend Way San Diego, CA 92121 United States

Contact

Tel: 1-858-455-9588
Fax: +49 (4131) 7023913

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Product Specifications
Scientific Background

Specifications

NameBiotin anti-human PCSK9 Antibody, PCSK9, Poly5250
Cat. No.525004
HostGoat
RRIDAB_2783339 (BioLegend Cat. No. 525004)
IsotypeGoat Polyclonal Ig
ReactivityHuman
ApplicationELISA Detection -Quality tested
ClonalityPolyclonal
Clone NumberPoly5250
Concentration0.5 mg/ml
TargetPCSK9
ImmunogenRecombinant protein
PurityThe antibody was purified by affinity chromatography and conjugated with biotin under optimal conditions.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
StorageThe antibody solution should be stored undiluted between 2°C and 8°C.Do not freeze.
Regulatory StatusResearch Use Only

Scientific Background

Proprotein convertase subtilisin/kexin 9 (PCSK9) belongs to the proteinase K subfamily of subtilases and is expressed as a soluble zymogen that undergoes autocatalytic intramolecular processing in the endoplasmic reticulum. It is a 692 amino acid (aa) glycoprotein with an overall domain structure similar to other proprotein convertase members. It is comprised of a signal peptide (aa 1–30), a pro segment (aa 31–152), a catalytic domain (aa 153–407), a hinge region (aa 408–452), and a C-terminal Cys-His-rich domain (aa 453–692).The biological roles of PCSK9 are closely related to its binding partners, low-density lipoprotein (LDL) and LDL receptor (LDLR). At the cell surface, secreted PCSK9 binds at a neutral pH to the EGF-A-like repeat of the LDLR via its catalytic domain. The binding of PCSK9 to LDLR enhances the degradation of the LDLR in endosomes/lysosomes, which results in increased circulating LDL-cholesterol (LDL-C). Thus, PCSK9 has gained attention as a pharmacological target for cardiovascular diseases and atherosclerosis. It also binds to the Apoliprotein B (ApoB) in LDL, although its role in this complex is not clearly understood. Due to the interaction of PCSK9 with LDLR, the levels of free PCSK9 or its complexed forms are important indicators for measuring risk of cardiovascular diseases or response to a therapy.

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