Recombinant Human Phospholipase A2 Group V (PLA2G5) Protein (His)

Name: Recombinant Human Phospholipase A2 Group V (PLA2G5) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10822P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Phospholipase A2 Group V (PLA2G5) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P39877
Target Symbol	PLA2G5
Synonyms	Ca2+ dependent phospholipase A2; Calcium dependent phospholipase A2; Calcium-dependent phospholipase A2; DKFZp686C2294; FRFB; Group V phospholipase A2; GV PLA2; gVPLA2; hVPLA(2); MGC46205; OTTHUMP00000044655; PA2G5_HUMAN; Phosphatidylcholine 2 acylhydrolase; Phosphatidylcholine 2-acylhydrolase 5; Phospholipase A2 group V; PLA2 10; PLA2 G5; PLA2-10; Pla2g5; sPLA2 Type V
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	GLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGTDWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKRNLRSYNPQYQYFPNILCS
Expression Range	21-138aa
Protein Length	Full Length of Mature Protein
Mol. Weight	15.6kDa
Research Area	Cardiovascular
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 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	HGNC: 9038 OMIM: 228980 KEGG: hsa:5322 STRING: 9606.ENSP00000364249 UniGene: Hs.319438
Associated Diseases	Fleck retina, familial benign (FRFB)
Tissue Specificity	Heart, placenta and less abundantly, in lung. Detected in the outer and inner plexiform layers of the retina (at protein level). Expressed in monocytes and macrophages.

Gene Functions References

Low GV-PLA2 expression is associated with cancer. PMID: 26715269
The clinical findings in this family suggest a diagnosis of benign familial fleck retina with excellent prognosis, in which the PLA2G5 gene may play a role. PMID: 25549071
sPLA2-V plays a thrombogenic role by impairing the ability of EPCR to promote protein C activation. PMID: 25069533
results demonstrate that EPCR is overexpressed and mediates the aggressive behavior of rheumatoid synovial fibroblasts, and is likely driven by group V secretory phospholipase A2 PMID: 24495480
expression of PLA2s-IIE and -V correlates with the development of calcification as well as the expression of pro-osteogenic molecules in human aortic valves PMID: 25132377
There is no association between rs525380 polymorphism of PLA2G5 and coronary heart disease. PMID: 24563418
Our results demonstrate the association of the PLA2G5 rs11573191 polymorphism with premature CAD. In our study, it was possible to distinguish one haplotype associated with increased risk of premature CAD and hypertension. PMID: 24959594
Human group V secretory phospholipase A2 is associated with lipid rafts and internalized in a flotillindependent pathway. PMID: 24042857
Our studies identified a unique function of gV-sPLA2 in activation of macrophages PMID: 23650617
The effects of acidic pH on the activity of recombinant human group V secreted phospholipase A(2) (sPLA(2)-V) toward small VLDL (sVLDL), IDL, and LDL, on the binding of these apoB-100-containing lipoproteins to human aortic proteoglycans, were examined. PMID: 22041135
Biallelic mutations in PLA2G5, encoding group V phospholipase A2, cause benign fleck retina PMID: 22137173
Group V phospholipase A2 mediates barrier disruption of human pulmonary endothelial cells caused by LPS in vitro PMID: 20448053
circulating human neutrophils express groups V and X sPLA(2) (GV and GX sPLA(2)) mRNA and contain GV and GX sPLA(2) proteins, whereas GIB, GIIA, GIID, GIIE, GIIF, GIII, and GXII sPLA(2)s are undetectable PMID: 11741884
group V phospholipase A2 induces group IVA phospholipase A2-independent cysteinyl leukotriene synthesis in human eosinophils PMID: 12796497
sPLA2-V expression in hepatocytes is induced by viral infection, fibrosis, and circulatory disturbance. Immunostaining using sPLA2-V antibody is useful for the detection of injured hepatocytes in patients with liver diseases. PMID: 15377291
foam cell formation is promoted by a SR-A- and CD36-independent process that involves cellular proteoglycans and Group V secretory phospholipase A2-modified low density lipoprotein PMID: 16040605
Group V sPLA2 was expressed in ischaemic cardiomyocytes around the lesion, while no expression was observed in normal heart. PMID: 16115226
present results raise the possibility that group V and X sPLA2s may play a role in innate immunity against adenoviral infection in the respiratory tract PMID: 16146426
group V PLA2 released from neighboring cells may function in triggering the activation of inflammatory cells under physiological conditions PMID: 16476735
Group V phospholipase A2, endogenously secreted from activated epithelial cells, promotes secretion of leukotriene C4 from cocultured eosinophils. PMID: 16785555
PLA2G5 tSNP haplotypes demonstrate an association with total and LDL cholesterol and oxLDL/LDL. PMID: 17545304

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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.

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