Recombinant Rat Phospholipase A2, Membrane Associated (PLA2G2A) Protein (His)

Name: Recombinant Rat Phospholipase A2, Membrane Associated (PLA2G2A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09650P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Rat Phospholipase A2, Membrane Associated (PLA2G2A) 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	P14423
Target Symbol	PLA2G2A
Synonyms	Pla2g2a; Phospholipase A2; membrane associated; EC 3.1.1.4; GIIC sPLA2; Group IIA phospholipase A2; Phosphatidylcholine 2-acylhydrolase 2A
Species	Rattus norvegicus (Rat)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	SLLEFGQMILFKTGKRADVSYGFYGCHCGVGGRGSPKDATDWCCVTHDCCYNRLEKRGCGTKFLTYKFSYRGGQISCSTNQDSCRKQLCQCDKAAAECFARNKKSYSLKYQFYPNKFCKGKTPSC
Expression Range	22-146aa
Protein Length	Full Length of Mature Protein
Mol. Weight	16.1kDa
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 with implications in host antimicrobial defense, inflammatory response and tissue regeneration. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response. Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner.
Subcellular Location	Secreted. Cell membrane; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein.
Protein Families	Phospholipase A2 family
Database References	KEGG: rno:29692 STRING: 10116.ENSRNOP00000022827 UniGene: PMID: 26162096 a novel inverse recruitment mechanism in which liganded TRbeta recruits corepressors to inhibit PLA2g2a expression. PMID: 23629656 Secreted PLA2-IIA regulates the permeability of microvascular endothelial cells during brain inflammation. PMID: 22788969 Data show changes in cell morphology and upregulation of ERK1/2, iNOS and sPLA-IIA expression in astrocytes and microglia on exposure to lipopolysaccharides and cytokines. PMID: 21943492 cPLA(2)alpha-mediated induction of PPAR-beta/delta is a novel intracellular signalling pathway in spontaneous and TGF-beta induced activation of hepatic stellate cells. PMID: 22093332 The expression of sPLA(2)-IIA in the dorsal horn and spinal trigeminal nucleus is consistent with previous results which showed an important role of CNS sPLA(2) in nociceptive transmission. PMID: 20153419 calcium-independent phospholipase A2beta has a role in high glucose-induced activation of RhoA, Rho kinase, and CPI-17 in cultured vascular smooth muscle cells and vascular smooth muscle hypercontractility in diabetic animals PMID: 20086008 During atherogenesis, SAA can amplify the involvement of smooth muscle cells in vascular inflammation and that this can lead to deposition of sPLA(2) and subsequent local changes in lipid homeostasis. PMID: 19850938 A calcium-independent, type IIA secretory phospholipase A2 newly isolated from liver mitochondria, most apparent in media of high ionic strength, initiates the removal of poorly functioning mitochondria by processes involving autolysis. PMID: 12056909 sPLA(2) may modulate neuronal COX-2 expression through mechanisms that differ from those of glutamate-induced COX-2 expression PMID: 12111798 analysed the activation of sPLA(2) transcription by cAMP and interleukin-1beta and showed that the 500 bp region upstream of the transcription start site of the sPLA(2) gene is implicated in activation by synergistically acting cAMP and IL-1beta PMID: 12188923 tumor necrosis factor alpha-induced secreted phospholipase A2 (sPLA2)-IIA expression is potentiated in mesangial cells by an autocrine loop involving sPLA2 and peroxisome proliferator-activated receptor alpha activation PMID: 12782627 Transcriptional activation of the group IIA secretory phospholipase A2 gene in vascular smooth muscle. PMID: 12882648 in a neonatal model, the development of an acidic surface pH can be ascribed, in part, to progressive stratum corneum acidification by two endogenous mechanisms, namely, sPLA2 and NHE1 PMID: 15009712 We investigated temporal and spatial expression of sPLA2-IIA mRNA and immunoreactivity in transient focal cerebral ischemia, demonstrating an up-regulation of the inflammatory sPLA2-IIA in reactive astrocytes in response to cerebral ischemia-reperfusion. PMID: 15255941 new autocrine and paracrine pathways activating sPLA2-IIA gene expression in rat and human vascular smooth muscle cells PMID: 15802623 12/15-LOX-dependent up-regulation of sPLA2-IIA expression may result from the interplay between accelerated MIP-2 signaling, AP-1 activation, and attenuated transforming growth factor-beta and platelet-derived growth factor signaling PMID: 15878884 the neuritogenic effect of sPLA2 is mediated by generation of LPC and subsequent activation of G2A PMID: 15927955 These results indicate that phospholipase A(2)-IIA is coexpressed with SNAP-25 in mature taste receptor cells that possess exocytotic machinery. PMID: 16385482 cytosolic and group IIA secreted phospholipases A(2) work together to liberate arachidonate from phospholipids in response to cytokines PMID: 16603549 HMGB1 slightly activated the sPLA2-IIA, COX-2, and mPGES-1 genes but dramatically stimulated these genes in VSMCs that had been incubated with the proinflammatory cytokine IL-1beta PMID: 16807371 It was shown that exposure of cultured astrocytes to oxygen glucose deprivation (0.5-24h) causes an increase in cPLA(2) and sPLA(2) expression and activity. PMID: 17462919 a novel regulatory role of iPLA(2)gamma in stimulus-coupled sPLA(2)-IIA expression. PMID: 17475622 On Chr 5, Pla2g2a is subject to a syntenic control while expression of the Tp53 (Chr 10) and Pmai1/Noxa (Chr 18) genes appears to be controlled by several mammary cancer resistance QTLs. PMID: 19052818 Simvastatin may reduce the process of atherosclerosis by decreasing the expression level of sPLA2 IIa in myocardium and aorta. PMID: 19237014 sPLA(2)-IIA may be an important mediator of oligodendrocyte death and a novel target for therapeutic intervention following spinal cord injury PMID: 19306380 Reactive oxygen species from NADPH oxidase iare involved in cytokine induction of sPLA2-IIA in astrocytes. Botanical antioxidants may be protective agents for inhibition of inflammatory responses in these cells. PMID: 19375465 sPLA2-derived oxidative products contribute to significant neurovascular damage, and treatment with sPLA2 inhibitor DEDA ameliorates secondary injury by reducing exacerbations from lipoxidative stress. PMID: 19678934

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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.