PLA2G2A Human

Secreted Phospholipase A2-IIA Human Recombinant
Cat. No.
BT21848
Source
Escherichia Coli.
Synonyms
MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, Phospholipase A2 membrane associated, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IIA phospholipase A2, GIIC sPLA2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, sPLA2-IIA, PLA2G2A.
Appearance

Filtered 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.
Shipped with Ice Packs
In Stock

Description

Secreted Phospholipase A2-IIA Human Recombinant is manufactured with N-terminal fusion of HisTag. PLA2G2A His-Tagged Fusion Protein is 15.8 kDa containing 124 amino acid residues of the human secreted phospholipase A2-IIA and 16 additional amino acid residues – HisTag.

Product Specs

Introduction
Phospholipase A2 (PLA2) enzymes catalyze the hydrolysis of membrane glycerophospholipids at the sn-2 position, releasing arachidonic acid (AA). AA serves as a precursor to eicosanoids, including prostaglandins and leukotrienes, which are potent inflammatory mediators. The reaction also generates lysophosholipids, another class of lipid mediators. The secretory PLA2 (sPLA2) family comprises ten identified isozymes, all of which are low-molecular-weight, calcium-dependent enzymes secreted by various cells. sPLA2s play roles in diverse biological processes, including eicosanoid production, inflammation, and host defense mechanisms. sPLA2 enzymes have been implicated in atherosclerosis, potentially by hydrolyzing phosphatidylcholine (PC) in lipoproteins within the arterial wall. This action releases lyso-PC and free fatty acids, contributing to the accumulation of bioactive lipids and modified lipoproteins within atherosclerotic plaques. Studies in mice highlight the role of sPLA2 in regulating HDL (high-density lipoprotein) particle size and composition. These studies indicate that sPLA2 activation is necessary for the reduction in plasma HDL cholesterol levels observed in response to inflammatory stimuli. Research in rats has shown that bacterial infection in the lungs leads to surfactant degradation, decreasing the ratio of large to small surfactant aggregates. This effect is associated with sPLA2 activity. sPLA2-IIA, a specific isoform of sPLA2, exhibits potent bactericidal properties, suggesting its beneficial role in combating infections. The production of sPLA2-IIA is typically triggered by endotoxin and a select group of cytokines through paracrine and/or autocrine signaling pathways.
Description
Recombinant Human Secreted Phospholipase A2-IIA is expressed with an N-terminal His-tag. This protein has a molecular weight of 15.8 kDa, comprising 124 amino acids of the human secreted phospholipase A2-IIA and a 16 amino acid His-tag.
Physical Appearance
Sterile filtered lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.5 mg/ml solution in 0.05M Acetate buffer, pH 4.
Purity
Purity is determined to be greater than 95% by SDS-PAGE analysis.
Solubility
To prepare a working stock solution of approximately 0.5 mg/ml, it is recommended to reconstitute the lyophilized pellet in 0.1M Acetate buffer, pH 4, ensuring complete dissolution. For use at higher pH, dilute the stock solution to 10 µg/ml using the appropriate buffer. Note: The solubility of PLA2G2A antigen is limited at higher concentrations. This product is not sterile; filter sterilize using an appropriate filter before use in cell culture.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the protein and store at -20°C to minimize freeze-thaw cycles. Reconstituted protein is stable at 4°C for up to two weeks with no observable changes.
Synonyms
MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, Phospholipase A2 membrane associated, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IIA phospholipase A2, GIIC sPLA2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, sPLA2-IIA, PLA2G2A.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASHMNLVN FHRMIKLTTG KEAALSYGFY GCHCGVGGRG SPKDATDRCC VTHDCCYKRL EKRGCGTKFL SYKFSNSGSR ITCAKQDSCR SQLCECDKAA ATCFARNKTT YNKKYQYYSN KHCRGSTPRC.

Product Science Overview

Structure and Function

sPLA2-IIA is a secreted enzyme with a His/Asp catalytic dyad, which means it uses histidine and aspartic acid residues in its active site to catalyze reactions . The enzyme is known for its high specificity for phospholipid substrates and its ability to function in extracellular environments .

Biological Roles

sPLA2-IIA plays a significant role in various physiological and pathological processes:

  1. Inflammation: sPLA2-IIA is an acute phase reactant, meaning its levels increase significantly during systemic inflammation. It has been implicated in inflammatory diseases such as rheumatoid arthritis and sepsis .
  2. Atherosclerosis: This enzyme is involved in the development of atherosclerosis by mediating monocyte recruitment and differentiation into antigen-presenting cells, which contribute to plaque formation in arteries .
  3. Innate and Adaptive Immunity: sPLA2-IIA acts as a mediator connecting innate and adaptive immune responses. It induces the differentiation of mononuclear cells and enhances their adhesive and migratory capabilities .
Clinical Significance

The gene encoding human sPLA2-IIA is located on chromosome 1p35 . Its expression is upregulated in various inflammatory conditions, making it a potential biomarker for diseases involving systemic inflammation . Additionally, sPLA2-IIA has been studied for its role in bacterial infections and its potential as a therapeutic target for inflammatory diseases .

Research and Applications

Research on sPLA2-IIA has expanded our understanding of its functions and mechanisms. Studies using knockout and transgenic mice have provided insights into the enzyme’s role in different pathophysiological conditions . Human recombinant sPLA2-IIA is used in research to study its enzymatic properties and potential therapeutic applications.

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