Recombinant Mouse Group 10 Secretory Phospholipase A2 (PLA2G10) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01981P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Group 10 Secretory Phospholipase A2 (PLA2G10) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01981P
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Product Overview

Description Recombinant Mouse Group 10 Secretory Phospholipase A2 (PLA2G10) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9QXX3
Target Symbol PLA2G10
Synonyms Group X secretory phospholipase A2 (GX sPLA2) (sPLA2-X) (Phosphatidylcholine 2-acylhydrolase 10)
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence GLLELAGTLDCVGPRSPMAYMNYGCYCGLGGHGEPRDAIDWCCYHHDCCYSRAQDAGCSPKLDRYPWKCMDHHILCGPAENKCQELLCRCDEELAYCLAGTEYHLKYLFFPSILCEKDSPKCN
Expression Range 29-151aa
Protein Length Full Length of Mature Protein
Mol. Weight 21.3 kDa
Research Area Metabolism
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 with preference for phosphatidylcholines and phosphatidylglycerols over phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty acyls. Contributes to phospholipid remodeling of very low-density lipoprotein (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells. Efficiently hydrolyzes and inactivates PAF, a potent lipid mediator present in oxidized LDL. May act in an autocrine and paracrine manner. Secreted by lung epithelium, targets membrane phospholipids of infiltrating eosinophils, releasing arachidonate and boosting eicosanoid and cysteinyl leukotriene synthesis involved in airway inflammatory response. Secreted by gut epithelium, hydrolyzes dietary and biliary phosphatidylcholines in the gastrointestinal lumen, thereby regulating adipogenesis and body weight. Plays a stem cell regulator role in colon epithelium. Within intracellular compartment, mediates Paneth-like cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates the Wnt signaling pathway in ISCs and tissue regeneration. May participate in hair follicle morphogenesis by regulating phosphatidylethanolamines metabolism at the outermost epithelial layer and facilitating melanin synthesis. By generating lysophosphatidylcholines (LPCs) at sperm acrosome controls sperm cell capacitation, acrosome reaction and overall fertility. May promote neurite outgrowth in neuron fibers involved in nociception. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. In pulmonary epithelium, may contribute to host defense response against adenoviral infection. Prevents adenovirus entry into host cells by hydrolyzing host cell plasma membrane, releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and viral infection. Likely prevents adenoviral entry into the endosomes of host cells. May play a role in maturation and activation of innate immune cells including macrophages, group 2 innate lymphoid cells and mast cells.
Subcellular Location Secreted. Lysosome. Cytoplasmic vesicle, secretory vesicle, acrosome.
Protein Families Phospholipase A2 family
Database References

KEGG: mmu:26565

STRING: 10090.ENSMUSP00000023364

UniGene: PMID: 27292189

  • PLA2G10 releases omega-3 polyunsaturated fatty acids, suppresses colitis, and promotes sperm fertility. PMID: 26828067
  • Progesterone-induced Acrosome Exocytosis Requires Sequential Involvement of Calcium-independent Phospholipase A2beta (iPLA2beta) and Group X Secreted Phospholipase A2 (sPLA2). PMID: 26655718
  • GX sPLA2 negatively regulated pancreatic insulin secretion by augmenting COX-2-dependent PGE2 production. PMID: 25122761
  • Mouse PLA2GX has a unique property of improving fertilization outcome among other secreted phospholipase A2 isoforms. PMID: 24287291
  • Data indicate that experimental allergic bronchitis (EAB) in was associated with increased expression of sPLA2, specifically sPLA2gX, in the lungs. PMID: 24204651
  • Authors propose that activation of GX-sPLA2 during H1N1pdm infection is an early step of pulmonary inflammation and its inhibition increases adaptive immunity and improves survival. PMID: 24725934
  • Pla2G10 limits the development of atherosclerosis in LDL receptor-null mice. PMID: 23349189
  • the use of a highly potent indole-based inhibitor of hGX-sPLA(2), RO061606 (which is ineffective against mGX-sPLA(2)), to assess the potential utility of GX-sPLA(2) blockade as a therapeutic intervention in asthma. PMID: 21652694
  • sPLA(2)-X in neutrophils plays a pathogenic role in abdominal aortic aneurysms in a mouse model. PMID: 21984544
  • sPLA2 plays a new role for fertilization by selecting a sperm subpopulation based on its effect on sperm motility. PMID: 21792918
  • Group X secretory phospholipase A2 promotes macrophage inflammatory responses by altering cellular cholesterol homeostasis and lipid raft content. PMID: 21622863
  • Physiological roles of group X-secreted phospholipase A2 in reproduction, gastrointestinal phospholipid digestion, and neuronal function. PMID: 21266581
  • the spatiotemporal expression of sPLA(2)-X in hair follicles, the presence of skin-specific machinery leading to sPLA(2)-X activation, a functional link of sPLA(2)-X with hair follicle homeostasis. PMID: 21266583
  • GX sPLA(2) promotes Ang II-induced pathological responses leading to abdominal aortic aneurysm formation PMID: 20833395
  • hydrolytic products generated by GX sPLA(2) negatively regulate adipogenesis, possibly by suppressing LXR activation PMID: 20585029
  • The overexpression of GX sPLA(2) significantly reduced ABCA1 and ABCG1 expression in J774 macrophage-like cells, whereas GX sPLA(2) deficiency in peritoneal macrophages was associated with enhanced expression. PMID: 20844270
  • Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice PMID: 20424324
  • LDL modification by GXPLA2 [GXPLA2] PMID: 12021277
  • group X secreted phospholipase A2 is expressed in neural cells and has neuritogenic action PMID: 15781456
  • sPLA2-X induces potent arachidonic acid release without activation of cytosolic phospholipase A2 alpha. PMID: 15789617
  • group V, but not group X, secreted phospholipase A2 has a role in lung dysfunction PMID: 17008322
  • direct attention to group X-secreted phospholipase A2 as a novel therapeutic target for asthma PMID: 17403936
  • Myocardial ischemia/reperfusion injury was attenuated in sPLA(2)-X(-/-) mice partly through the suppression of neutrophil cytotoxic activities PMID: 18506007
  • secretory phospholipase A2 group X enhances anti-inflammatory responses, promotes lipid accumulation, and contributes to aberrant lung pathology PMID: 18511424
  • Enhanced protein expression in mammalian cells using engineered SUMO fusions: example of secreted PLA2-X. PMID: 18539905
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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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