Analytical Data
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Gene name
PISD
- Application
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Alternative Names
PISD；Phosphatidylserine decarboxylase proenzyme. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UG56
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Expression Region
1-375aa
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AA Sequence
MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGALRPLSRVGWRPVSRVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
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Molecular Weight
56.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Pseudomonas aeruginosa is a common opportunistic pathogen responsible for various infections, particularly in immunocompromised patients. One of the key factors contributing to its virulence is the presence of proteinase inhibitors, such as PISD (Pseudomonas Inhibitor of Serine Proteases D), which play a significant role in the bacterium's ability to evade host immune responses. Research on the PISD protein has gained traction due to its potential utility in therapeutic applications and as a target for novel antimicrobial strategies. Understanding the structure, function, and mechanisms of PISD can provide insights into its role in bacterial pathogenicity and immune evasion. Studies have demonstrated that PISD can inhibit various serine proteases, which are crucial in the activation of immune pathways. By exploring the biochemical properties and interactions of PISD with its substrates, researchers aim to elucidate the molecular pathways involved in bacterial resistance, which may pave the way for the development of innovative treatments against Pseudomonas infections. Moreover, characterizing PISD's structure could lead to the design of specific inhibitors that may assist in enhancing host defense mechanisms or restoring susceptibility to conventional antibiotics. This area of research is particularly relevant in the context of rising antibiotic resistance, making the exploration of protein-based approaches to combat infections a pressing imperative in modern medicine. Consequently, PISD not only serves as a fascinating subject for fundamental microbiological research but also represents a promising avenue for translational applications in the fight against antibiotic-resistant pathogens.
