Recombinant Mouse Calcium-Dependent Phospholipase A2 (PLA2G5) Protein (His-SUMO)

Name: Recombinant Mouse Calcium-Dependent Phospholipase A2 (PLA2G5) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03118P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Calcium-Dependent Phospholipase A2 (PLA2G5) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P97391
Target Symbol	PLA2G5
Synonyms	Pla2g5; Calcium-dependent phospholipase A2; EC 3.1.1.4; Group V phospholipase A2; PLA2-10; Phosphatidylcholine 2-acylhydrolase 5
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	GLLELKSMIEKVTGKNAFKNYGFYGCYCGWGGRGTPKDGTDWCCQMHDRCYGQLEEKDCAIRTQSYDYRYTNGLVICEHDSFCPMRLCACDRKLVYCLRRNLWTYNPLYQYYPNFLC
Expression Range	21-137aa
Protein Length	Full Length of Mature Protein
Mol. Weight	29.8kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), preferentially releasing fatty acyl groups with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl (C18:2) groups. Hydrolyzes low-density lipoprotein (LDL) phospholipids releasing unsaturated fatty acids that drive macrophage polarization toward an M2 phenotype. May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes at different subcellular locations and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of cardiolipin, a major component of the inner membrane of mitochondria and bacterial membranes. Promotes phagocytosis of bacteria in macrophages through production of lysophosphatidylethanolamines. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing the phospholipids of the bacterial membrane. Promotes phagocytosis and killing of ingested fungi likely through controlling phagosome-lysosome fusion and phagosome maturation. Plays a role in biosynthesis of cysteinyl leukotrienes (CysLTs) in myeloid cells. In eosinophils, triggers perinuclear arachidonate release and LTC4 synthesis in a PLA2G4A-independent way. In neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A. Promotes immune complex clearance in macrophages via stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger phagocytosis. May regulate antigen processing in antigen-presenting cells. In pulmonary macrophages regulates IL33 production required for activation of group 2 innate lymphoid cells. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines.
Subcellular Location	Secreted. Cell membrane. Cytoplasmic vesicle, phagosome. Recycling endosome. Golgi apparatus, cis-Golgi network. Golgi apparatus, trans-Golgi network.
Protein Families	Phospholipase A2 family
Database References	KEGG: mmu:18784 STRING: 10090.ENSMUSP00000030524 UniGene: PMID: 29346348 Deficiency of GV sPLA2 results in diminished glucose-stimulated insulin secretion in isolated pancreatic beta-cells PMID: 28825176 GV sPLA2 is involved in the maintenance of tubular cell function and integrity, promoting sodium retention through increased cortical (Na+ + K+)-ATPase expression and activity. PMID: 26820468 AdPLA2 plays an important role in promoting tumorigenesis and disease progression by modulating the production of prostaglandins and may serve as a potential therapeutic target in TSC and LAM. PMID: 25347447 PLA2G5 hydrolyzed phosphatidylcholine in fat-overladen low-density lipoprotein to release unsaturated fatty acids, which prevented palmitate-induced M1 macrophage polarization. PMID: 24910243 Key Data shows the role of group v secreted phospholipase A2 in Th2 cytokine and dendritic cell-driven airway hyperresponsiveness and remodeling. PMID: 23451035 Our studies identified a unique function of gV-sPLA2 in activation of macrophages PMID: 23650617 The impact of group V sPLA(2) deficiency on angiotensin (Ang) II-induced cardiac fibrosis in apoE deficient mice was investigated. PMID: 22813854 The results indicate that the PLA(2) activity also plays a substantial role in protecting cells against oxidant stress caused by an exogenous hydroperoxide. PMID: 22067043 GV sPLA(2) in bone marrow-derived myeloid cells as well as non-myeloid cells, which are likely bronchial epithelial cells, participate in the regulation of the innate immune response to pulmonary infection with E. coli. PMID: 21849511 Data from cuprizone-induced model of multiple sclerosis suggest that sPLA2 down-regulation during remyelination can limit release of AA and consequent production of pro-inflammatory PGs/TXB2 (which are increased during demyelination). PMID: 21530210 sPLA(2)-V plays an important role in the pathogenesis of myocardial ischemia reperfusion injury partly in concert with the activation of cPLA(2) PMID: 21169294 agonist-induced MAPK activation leads to Prdx6 phosphorylation and translocation to the cell membrane, where its PLA(2) activity facilitates assembly of the NOX2 complex and activation of the oxidase. PMID: 21262967 expression of group V sPLA(2) in antigen-presenting cells regulates Ag processing and maturation of dendritc cells and contributes to pulmonary inflammation and immune response against D. farinae. PMID: 20817863 Demonstrate the role of sPLA(2)-V in lipopolysaccharide-induced ICAM-1 and VCAM-1 protein overexpression and leukocyte recruitment, supporting the contribution of sPLA(2)-V in the development of inflammatory innate immune responses. PMID: 20232296 encapsulation of Group V PLA2 into granules brings the enzyme to the perinuclear envelope during cell activation PMID: 12963740 a role in innate immunity. PMID: 14761945 Group V secretory PLA2 contributes to the innate immune response both through regulation of eicosanoid generation in response to a phagocytic stimulus and also as a component of the phagocytic machinery. PMID: 16407308 group V, but not group X, secreted phospholipase A2 has a role in lung dysfunction PMID: 17008322 Delayed-phase PGD(2) generation and COX-2 induction were reduced approximately 35% in C57BL/6 Pla2g5-/- bone marrow-derived mast cells. PMID: 17064958 In mast cells lacking group V secretory PLA(2), the course of phosphorylation of ERK1/2 and of cPLA(2)alpha was markedly truncated. PMID: 17369491 group v phospholipase A2 is a critical messenger enzyme in the development of airway hyperresponsiveness and regulation of cell migration during immunosensitization by a pathway that is independent of group IVa phospholipase A2 PMID: 17878379 results demonstrate the critical role of cPLA2 for the duration of inflammation in collagen-induced arthritis PMID: 18825749 role for syndecan-4 in mediating the uptake of LDL modified by group V secretory phospholipase A2, a process implicated in atherosclerotic lesion progression PMID: 19056705 sPLA(2), either through pathways comprising Ras/Raf-1/MEK1/ERK1/2 or the classical PKC family, plays an essential role in Mtb-mediated ROS generation and inflammatory mediator release by microglial cells. PMID: 19115385 gVPLA(2) is an inducible protein in pla2g5(+/+) mice but not in pla2g5(-/-) mice within 24 h after lipopolysaccharide treatment PMID: 19286925 group V sPLA(2) regulates phagocytosis through major phagocytic receptors and contributes to the innate immune response against C. albicans by regulating phagocytosis and killing through a mechanism that is likely dependent on phagolysosome fusion PMID: 19342668

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.