HRAS-Like Suppressor 3 Human Recombinant (PLA2G16)
Secreted Phospholipase A2-X Human Recombinant
Secreted Phospholipase A2-X Human Recombinant is manufactured with N-terminal fusion HisTag. PLA2G10 His-Tagged Fusion Protein, is 15.5 kDa containing 123 amino acid residues of the human secreted phospholipase A2-X and 16 additional amino acid residues - HisTag (underlined).
Secreted Phospholipase A2-XII Human Recombinant
Secreted Phospholipase A2-IB Human Recombinant
Secreted Phospholipase A2-IIA Human Recombinant
Filtered lyophilized (freeze-dried) powder.
Secreted Phospholipase A2-IID Human Recombinant
Secreted Phospholipase A2-IIE Human Recombinant
Secreted Phospholipase A2-IIE Human Recombinant manufactured with N-terminal His-Tag. PLA2G2E His-Tagged Fusion Protein is 15.8 kDa protein containing 123 amino acid residues of the human secreted phospholipase A2-IIE and 16 additional amino acid residues – His-Tag (underlined).
Secreted Phospholipase A2-V Human Recombinant
Secreted Phospholipase A2-VII Human Recombinant
Secreted Phospholipase A2-VII Human Recombinant, HEK
Secreted Phospholipase A2 (sPLA2) is a member of the phospholipase A2 superfamily, which comprises enzymes that hydrolyze the sn-2 acyl bond of glycerophospholipids to release fatty acids and lysophospholipids . sPLA2 enzymes are characterized by their low molecular weight, requirement for calcium ions (Ca²⁺) for activity, and a conserved His/Asp catalytic dyad . They are classified into several groups based on their structure and function, including groups IB, IIA, IIC, IID, IIE, IIF, III, V, X, XIIA, and XIIB .
sPLA2 enzymes exhibit distinct biological properties, including specific expression patterns and tissue distribution. They are found in various mammalian tissues, such as the pancreas, kidney, and central nervous system . sPLA2 enzymes are also present in snake and insect venoms . Their expression can be induced during inflammation, and they play roles in metabolic regulation, including lipid metabolism and energy production .
The primary biological functions of sPLA2 include the hydrolysis of phospholipids to produce fatty acids and lysophospholipids, which serve as precursors for bioactive lipid mediators such as prostaglandins and leukotrienes . sPLA2 enzymes are involved in immune responses, pathogen recognition, and host defense mechanisms . They contribute to inflammation, atherosclerosis, and other pathophysiological processes .
sPLA2 enzymes interact with other molecules and cells through various mechanisms. They bind to specific receptors on cell surfaces, leading to the activation of downstream signaling cascades . The hydrolysis of phospholipids by sPLA2 results in the release of arachidonic acid, which is further metabolized into eicosanoids, potent mediators of inflammation . sPLA2 enzymes also modulate membrane composition and participate in lipid signaling .
The expression and activity of sPLA2 are tightly regulated by multiple mechanisms. Transcriptional regulation involves the activation of specific genes in response to inflammatory stimuli . Post-translational modifications, such as phosphorylation, can modulate the enzyme’s activity and localization . Calcium ions are essential for the catalytic activity of sPLA2, and their concentration can influence enzyme function .
sPLA2 enzymes have various applications in biomedical research, diagnostic tools, and therapeutic strategies. They are used as biomarkers for inflammatory diseases and cancer . Inhibitors of sPLA2 are being developed as potential therapeutic agents for conditions such as acute lung injury and atherosclerosis . sPLA2 enzymes are also studied for their roles in lipid metabolism and energy homeostasis .
sPLA2 enzymes play crucial roles throughout the life cycle, from development to aging and disease. During development, they are involved in processes such as sperm maturation and capacitation . In adulthood, sPLA2 enzymes contribute to immune responses and metabolic regulation . In aging and disease, their dysregulation is associated with inflammatory conditions, metabolic disorders, and cancer .