Analytical Data
-
Gene name
PAFAH2
- Application
-
Alternative Names
PAFAH2;Platelet-activating factor acetylhydrolase 2. cytoplasmic
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q99487
-
Expression Region
1-392aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMGVNQSVGFPPVTGPHLVGCGDVMEGQ NLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCTGLAEYLQFNKRCGGLLF NLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAFCMELASR GFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKE FHVRNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDM SRVAVMGHSFGGATAILALAKETQFRCAVALDAWMFPLERDFYPKARGPV FFINTEKFQTMESVNLMKKICAQHEQSRIITVLGSVHRSQTDFAFVTGNL IGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKHLDLKEDYNQWNNLIEGI GPSLTPGAPHHLSSL
-
Molecular Weight
46 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PAFAH2, also known as phospholipase A2 family member 2, is an enzyme that plays a significant role in lipid metabolism and inflammation regulation. Given its involvement in the hydrolysis of phospholipids, PAFAH2 has garnered attention for its potential implications in various pathological conditions, including cardiovascular diseases and cancer. Research has shown that dysregulation of phospholipid metabolism can contribute to the progression of these diseases, which underscores the importance of understanding PAFAH2's structure, function, and regulatory mechanisms. Recent studies have focused on the recombinant expression of PAFAH2 to facilitate detailed biochemical characterization and functional assays. By producing PAFAH2 as a recombinant protein, researchers aim to investigate its enzymatic properties, interactions with other cellular components, and its role in mediating inflammatory responses. The recombinant approach allows for the production of large quantities of pure enzyme, enabling in vitro studies to elucidate its substrate specificity and inhibition mechanisms. Furthermore, exploring the potential of PAFAH2 as a therapeutic target may open new avenues for treating diseases associated with lipid dysregulation. Overall, advances in the recombinant technology surrounding PAFAH2 could provide critical insights into its biological functions and therapeutic applications, highlighting its relevance in the growing field of lipidomics and disease modulation.
