PLA2G7 Human, HEK

Secreted Phospholipase A2-VII Human Recombinant, HEK
Cat. No.
BT22266
Source
HEK293 cells.
Synonyms
Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SEC-HPLC and SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Human PLA2G7 produced in HEK293 cells is a polypeptide chain (22-441 a.a), fused to an 8 amino acid His-tag at C-terminus, containing a total of 428 amino acids.
PLA2G7 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PLA2G7, a secreted enzyme, plays a crucial role in degrading platelet-activating factor (PAF) into inactive forms. Primarily produced by inflammatory cells, PLA2G7 hydrolyzes oxidized phospholipids within LDL. In the bloodstream, it predominantly associates with LDL, with less than 20% bound to HDL. PLA2G7 has been implicated in atherosclerosis development and serves as a cardiac disease marker. It potentially exerts significant physiological influence during inflammatory responses. By hydrolyzing the sn-2 ester bond in PAF, PLA2G7 generates the inactive lyso-PAF, effectively modulating PAF's activity. This enzyme exhibits specificity towards substrates possessing a short residue at the sn-2 position, remaining inactive against long-chain phospholipids. Genetic defects in PLA2G7 can lead to platelet-activating factor acetylhydrolase deficiency, a characteristic observed in 27% of the Japanese population.
Description
Recombinant Human PLA2G7, expressed in HEK293 cells, is a polypeptide chain encompassing amino acids 22-441. An 8 amino acid His-tag is fused to the C-terminus, resulting in a total of 428 amino acids. The purification of PLA2G7 is achieved using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
PLA2G7 is provided as a 0.2µm filtered solution prepared in a buffer consisting of 20mM HAc-NaCl, 150mM NaCl, and 10% Glycerol, at a pH of 4.5.
Stability
For optimal storage, keep at 4°C if the entire vial is intended for use within 2-4 weeks. For extended storage, freeze at -20°C. Repeated freezing and thawing cycles should be avoided.
Purity
High purity exceeding 95%, as determined by SEC-HPLC and SDS-PAGE analyses.
Synonyms
Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.
Source
HEK293 cells.
Amino Acid Sequence
FDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGNGPYSVGCTDLMFDHTNKGTFLRLYYPS
QDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNILRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGL
GAFRTLYSAIGIDLASHGFIVAAVEHRDRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRN
EQVRQRAKECSQALSLILDIDHGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSE
DQRFRCGIALDAWMFPLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVH
QNFADFTFATGKIIGHMLKLKGDIDSNAAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLI
PGTNINTTNQHIMLQNSSGIEKYNVDHHHHHH.

Product Science Overview

Introduction

Secreted Phospholipase A2-VII (sPLA2-VII), also known as Platelet-Activating Factor Acetylhydrolase (PAF-AH), is an enzyme encoded by the PLA2G7 gene in humans. This enzyme is part of the secreted phospholipases A2 (sPLA2) family, which plays a crucial role in lipid metabolism and inflammatory processes.

Structure and Function

sPLA2-VII is a secreted enzyme that hydrolyzes the sn-2 ester bond of phospholipids, releasing free fatty acids and lysophospholipids. This hydrolytic activity is essential for the degradation of platelet-activating factor (PAF) and oxidized phospholipids in low-density lipoproteins (LDL), converting them into biologically inactive products . The enzyme is primarily produced by inflammatory cells and circulates in the blood, predominantly associated with LDL and to a lesser extent with high-density lipoproteins (HDL) .

Biological Significance

The primary biological function of sPLA2-VII is to modulate inflammatory responses. By degrading PAF, a potent inflammatory mediator, sPLA2-VII helps regulate inflammation and immune responses. Additionally, the enzyme’s ability to hydrolyze oxidized phospholipids in LDL is crucial for preventing the formation of atherosclerotic plaques, thereby playing a protective role against cardiovascular diseases .

Expression and Tissue Distribution

sPLA2-VII is expressed in various tissues, with high expression levels observed in the liver, kidney, and heart. The enzyme is also present in inflammatory cells such as macrophages and neutrophils, where it contributes to the regulation of inflammatory processes .

Recombinant Production

The recombinant form of sPLA2-VII, produced in Human Embryonic Kidney (HEK) cells, is widely used in research to study its structure, function, and role in various diseases. The recombinant enzyme retains the same biological activity as the native enzyme, making it a valuable tool for biochemical and pharmacological studies .

Clinical Implications

Given its role in modulating inflammation and preventing atherosclerosis, sPLA2-VII is a potential therapeutic target for treating inflammatory diseases and cardiovascular disorders. Inhibitors of sPLA2-VII are being explored as potential therapeutic agents to reduce inflammation and prevent the progression of atherosclerosis .

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