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Recombinant Pig Phospholipase A2, major isoenzyme (PLA2G1B)

Recombinant Pig Phospholipase A2, major isoenzyme (PLA2G1B)

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

PLA2G1B

Uniprot NO.

P00592

Alternative Names

PLA2G1B; Phospholipase A2; major isoenzyme; EC 3.1.1.4; Group IB phospholipase A2; Phosphatidylcholine 2-acylhydrolase 1B

Species

Sus scrofa (Pig)

Source

Yeast

Expression Region

23-146

Target Protein Sequence

ALWQFRSM IKCAIPGSHP LMDFNNYGCY CGLGGSGTPV DELDRCCETH DNCYRDAKNL DSCKFLVDNP YTESYSYSCS NTEITCNSKN NACEAFICNC DRNAAICFSK APYNKEHKNL DTKKYC
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 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.

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Target Background

Function(From Uniprot)

Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. 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. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. May act in an autocrine and paracrine manner. Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity.

Gene References into Functions

Equilibrium unfolding of porcine pancreatic phospholipase A2 was monitored using multiple approaches. An unusually broad unfolding transition at remarkably high denaturant concentration was observed. PMID:26117657
Porcine group IB secretory phospholipase A2 (PLA2G1B) stimulates the expression and secretion of CXC chemokine ligand 8 (CXCL8) in human neutrophils without affecting other proinflammatory cytokines. PMID:15528384
Porcine pancreatic PLA(2) shows a long lag phase of several hours during which the enzyme binds to the bilayer surface, but only 5+/-3% of the lipids react before the onset of rapid hydrolysis. PMID:17355873
Results describe the structural basis for bile salt inhibition of pancreatic phospholipase A2. PMID:17434532
MMP-2/9 production is regulated by sPLA2-IB acting as a receptor ligand to activate cPLA2 PMID:17981679
Results show that the decylsulfate epitope for the successive E i (#) complexes increasingly resembles the micellar complex formed by the binding of PLA2 to preformed micelles. PMID:18260608
An increased sPLA(2) activity and a reduced inhibition may play an important role in the pathogenesis of ischemia-reperfusion injury of non-heart-beating donor liver grafts. PMID:18468626
Interfacial activation of pig pancreatic IB phospholipase A(2) (PLA2) is modeled in terms of the three discrete premicellar complexes (E(i)(#), i = 1, 2, or 3) consecutively formed by the cooperative binding of a monodisperse amphiphile to the i-face PMID:19301847