Analytical Data
-
Gene name
PIGL
- Application
-
Alternative Names
PIGL；N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y2B2
-
Expression Region
1-252aa
-
AA Sequence
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPTVLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGMQWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVLTLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIFSRYMRINSLSFL
-
Molecular Weight
28.5 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
PIGL (Phosphatidylinositol Glycan Anchor Biosynthesis Class L) is a key enzyme involved in the biosynthesis of glycosylphosphatidylinositol (GPI) anchors, which are essential for the proper localization and function of various proteins in eukaryotic cells. The significance of PIGL stems from its role in modifying the GPI anchor structure, which is crucial for protein attachment to the cell membrane and plays a vital role in various cellular processes, including signaling and interactions with the extracellular matrix. Mutations in the PIGL gene have been linked to several human disorders, including hyperphosphatasia with mental retardation syndrome, highlighting the clinical relevance of understanding its function and regulation. Research into PIGL and its recombinant protein forms aims to elucidate the enzyme's catalytic mechanisms, explore potential therapeutic interventions for associated diseases, and develop novel biotechnological applications. By studying PIGL's structure-function relationships, scientists hope to uncover insights that can lead to new strategies for manipulating GPI anchor biosynthesis in various biomedical contexts, ultimately contributing to advances in targeted therapies and the treatment of genetic disorders.
