PLA2G12 Human

Secreted Phospholipase A2-XII Human Recombinant
Cat. No.
BT21695
Source
Escherichia Coli.
Synonyms
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95% as determined by 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.
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Description

Secreted Phospholipase A2-XII Human Recombiannt was produced with N-terminal His-Tag. PLA2G12 His-Tagged Fusion Protein is 20.6 kDa containing 167 amino acid residues of the human secreted phospholipase A2-XII and 16 additional amino acid residues – His-Tag (underlined).

Product Specs

Introduction
Phospholipase A2 (PLA2) enzymes play a crucial role in hydrolyzing glycerophospholipids at the sn-2 position, releasing arachidonic acid (AA). AA serves as a precursor for eicosanoids, including prostaglandins and leukotrienes, which are involved in inflammation and other biological processes. The reaction also generates lysophosholipids, another class of lipid mediators. The secretory PLA2 (sPLA2) family comprises ten identified isozymes, which are low molecular weight, Ca2+-dependent enzymes secreted by cells. sPLA2s have been implicated in various biological functions, including modulating eicosanoid production, inflammation, and host defense mechanisms. Studies suggest that sPLA2 may contribute to atherosclerosis by hydrolyzing phosphatidylcholine (PC) in lipoproteins within the arterial wall, leading to the release of lyso-PC and free fatty acids, which can accumulate and contribute to the formation of atherosclerotic plaques. Research in mice indicates that sPLA2 expression significantly affects HDL particle size and composition. Furthermore, sPLA2 induction appears necessary for the reduction of plasma HDL cholesterol in response to inflammatory stimuli. In rats, bacterial instillation into the bronchi has been linked to surfactant degradation and a decrease in the large:small ratio of surfactant aggregates.
Description
Recombinant human secreted Phospholipase A2-XII was produced with an N-terminal His-Tag. The PLA2G12 His-Tagged Fusion Protein has a molecular weight of 20.6 kDa and consists of 167 amino acid residues from the human secreted phospholipase A2-XII protein and an additional 16 amino acid residues comprising the His-Tag (underlined).
Physical Appearance
White lyophilized powder, filtered for purity.
Formulation
The protein was filtered through a 0.4 μm filter and lyophilized from a solution containing 0.5 mg/ml protein in 0.01M Tris buffer at pH 8.6.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized pellet to achieve a concentration of approximately 0.5 mg/ml. Allow the pellet to dissolve completely. Please note that this product is not sterile. Before using it for cell culture, filter the solution through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the protein to avoid repeated freeze-thaw cycles. The reconstituted protein can be stored at 4°C for a limited period. No significant changes in protein quality were observed after storage at 4°C for two weeks.
Purity
The purity of the protein is greater than 95% as determined by SDS-PAGE analysis.
Applications
This product is suitable for use in Western blotting applications.
Synonyms
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASHMQEQA QTTDWRATLK TIRNGVHKID TYLNAALDLL GGEDGLCQYK CSDGSKPFPR YGYKPSPPNG CGSPLFGVHL NIGIPSLTKC CNQHDRCYET CGKSKNDCDE EFQYCLSKIC RDVQKTLGLTQ HVQACETTVE LLFDSVIHLG CKPYLDSQRA ACRCHYEEKT DL

Product Science Overview

Introduction

Secreted Phospholipase A2 (sPLA2) enzymes are a diverse group of enzymes that play crucial roles in various biological processes. Among the different isoforms, Secreted Phospholipase A2-XII (sPLA2-XII) is particularly interesting due to its unique properties and functions. This article delves into the background, structure, function, and significance of sPLA2-XII, with a focus on its human recombinant form.

Structure and Classification

Phospholipase A2 (PLA2) enzymes catalyze the hydrolysis of the sn-2 position of glycerophospholipids, resulting in the release of fatty acids and lysophospholipids . The sPLA2 family is characterized by low molecular weight, calcium dependency, and a conserved His-Asp catalytic dyad . sPLA2-XII is one of the 11 isoforms identified in mammals, each exhibiting unique distributions and specific enzymatic properties .

Biological Functions

sPLA2-XII, like other sPLA2 enzymes, is involved in the metabolism of phospholipids, leading to the production of bioactive lipid mediators such as prostaglandins and leukotrienes . These mediators play significant roles in inflammation, atherosclerosis, and other metabolic disorders . The enzyme’s ability to hydrolyze phospholipids also implicates it in various cellular processes, including membrane remodeling and signal transduction .

Physiological and Pathological Roles

Recent studies have highlighted the diverse roles of sPLA2-XII in both physiological and pathological contexts. For instance, sPLA2-XII has been implicated in the regulation of metabolic disorders such as obesity, hepatic steatosis, diabetes, and insulin resistance . Its involvement in inflammation and atherosclerosis has also been well-documented, with evidence suggesting that sPLA2-XII contributes to the formation of pro-atherogenic low-density lipoprotein (LDL) and macrophage foam cell formation .

Human Recombinant sPLA2-XII

The recombinant form of sPLA2-XII is produced using advanced biotechnological methods, allowing for the study of its structure and function in detail. Human recombinant sPLA2-XII is particularly valuable for research purposes, as it provides insights into the enzyme’s role in various biological processes and potential therapeutic applications.

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