Analytical Data
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Gene name
PIGH
- Application
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Alternative Names
PIGH; Phosphatidylinositol N-acetylglucosaminyltransferase subunit H; EC 2.4.1.198; Phosphatidylinositol-glycan biosynthesis class H protein; PIG-H
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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
Q14442
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Expression Region
1-188 aa
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AA Sequence
MEDERSFSDI CGGRLALQRR YYSPSCREFC LSCPRLSLRS LTAVTCTVWL AAYGLFTLCE NSMILSAAIF ITLLGLLGYL HFVKIDQETL LIIDSLGIQM TSSYASGKES TTFIEMGKVK DIVINEAIYM QKVIYYLCIL LKDPVEPHGI SQVVPVFQSA KPRLDCLIEV YRSCQEILAH QKATSTSP
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Molecular Weight
21.0 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
PIGH (Phosphatidylinositol glycan anchor biosynthesis class H) is a pivotal enzyme involved in the biosynthesis of glycosylphosphatidylinositol (GPI) anchors, which are essential for the attachment of proteins to cell membranes. The study of PIGH-recombinant proteins is primarily driven by the importance of GPI anchors in various biological processes, including cell signaling, membrane structure, and the immune response. Alterations in GPI anchor biosynthesis are implicated in several human diseases, such as cancer, neurodegenerative disorders, and congenital disorders of glycosylation. The recombinant expression of PIGH allows researchers to investigate its structure-function relationship and its role in GPI biosynthesis more thoroughly. Understanding the functional mechanisms of PIGH and its interactions with other components of the GPI biosynthetic pathway can provide insights into the pathological mechanisms of various diseases linked to GPI anchors. Furthermore, the production of PIGH-recombinant proteins facilitates the screening of potential therapeutic targets and the development of treatments aimed at correcting GPI anchor deficiencies. Thus, research on PIGH-recombinant proteins is crucial for advancing our knowledge of glycosylation processes and their implications in health and disease.
