Recombinant Human PISD GST (N-Term) Protein Summary
Description |
A recombinant protein with GST tag at N-terminal corresponding to the amino acids 1-409 of Human PISD Source: Wheat Germ (in vitro) Amino Acid Sequence: MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL |
Preparation Method |
in vitro wheat germ expression system |
Details of Functionality |
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated. |
Source |
Wheat germ |
Protein/Peptide Type |
Recombinant Protein |
Gene |
PISD |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- ELISA
- Immunoaffinity Purification
- Protein Array
- SDS-Page
- Western Blot
|
Theoretical MW |
71.39 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -80C. Avoid freeze-thaw cycles. |
Buffer |
50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0 in the elution buffer. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Notes
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Recombinant Human PISD GST (N-Term) Protein
Background
PISD, also referred to as Phosphatidylserine Decarboxylase proenzyme, is cleaved into two mature subunits called Phosphatidylserine decarboxylase alpha chain and Phosphatidylserine decarboxylase beta chain. The PISD proenzyme contains a LGST motif that is an autocatalytic cleavage site where it splits into the alpha chain and beta chain. PISD is part of the phosphatidylserine decarboxylase family and localizes to the mitochondrion. Current research on PISD is being conducted in relation to several diseases and disorders including carcinomas and malaria. Research has shown that PISD interacts with PMM2, SGPL1, DHX29, CRLS1 and NAPEPLD in pathways such as the FOXA1 transcription factor network, the metabolism of lipids and lipoproteins and glycerophospholipid metabolism.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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