PIGS
- Product List
- Overview
- Review / Q&A
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Official Full Name
phosphatidylinositol glycan anchor biosynthesis, class S -
Overview
This gene encodes a protein that is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI) anchor;is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene encodes an;essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the;endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. -
Synonyms
PIGS;phosphatidylinositol glycan anchor biosynthesis, class S;GPI transamidase component PIG-S;DKFZp686K20216;FLJ45226;GPI transamidase subunit;Phosphatidylinositol glycan anchor biosynthesis class S;Phosphatidylinositol glycan class S;Phosphatidylinositol-glycan biosynthesis class S protein;PIGS_HUMAN;phosphatidylinositol glycan, class S homolog;Gm393;Gm689;BC058979
Recombinant Proteins
- Human
- Rat
- Zebrafish
- Bovine
- Mus musculus
- E.coli
- Mammalian Cells
- HEK293
- His
- Avi
- Fc
Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
PIGS-1710H | Recombinant Human PIGS, His-tagged | E.coli | Human | His | C-term-243aa | |
PIGS-4451R | Recombinant Rat PIGS Protein | Mammalian Cells | Rat | His |
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PIGS-4507Z | Recombinant Zebrafish PIGS | Mammalian Cells | Zebrafish | His |
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PIGS-4111R | Recombinant Rat PIGS Protein, His (Fc)-Avi-tagged | HEK293 | Rat | Avi&Fc&His |
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RFL15138BF | Recombinant Full Length Bovine Gpi Transamidase Component Pig-S(Pigs) Protein, His-Tagged | E.coli | Bovine | His | Full L. Full Length of Mature Protein (2-555) |
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RFL18912RF | Recombinant Full Length Rat Gpi Transamidase Component Pig-S(Pigs) Protein, His-Tagged | E.coli | Rat | His | Full L. Full Length of Mature Protein (2-555) |
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RFL35369HF | Recombinant Full Length Human Gpi Transamidase Component Pig-S(Pigs) Protein, His-Tagged | E.coli | Human | His | Full L. Full Length of Mature Protein (2-555) |
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RFL5735MF | Recombinant Full Length Mouse Gpi Transamidase Component Pig-S(Pigs) Protein, His-Tagged | E.coli | Mus musculus | His | Full L. Full Length of Mature Protein (2-555) |
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Involved Pathway
PIGS involved in several pathways and played different roles in them. We selected most pathways PIGS participated on our site, such as Glycosylphosphatidylinositol(GPI)-anchor biosynthesis,Metabolic pathways, which may be useful for your reference. Also, other proteins which involved in the same pathway with PIGS were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Glycosylphosphatidylinositol(GPI)-anchor biosynthesis | PIGF,PIGU,PIGH,GPAA1,PIGQ,PIGM,PIGL,PIGYL,PIGA,PIGZ |
Metabolic pathways | GCSH,UGT8A,PIGN,MLYCD,GMPPAB,NME2B.1,CYP2J6,ATP6V1B2,CYP11B1,ALDOAA |
Protein Function
PIGS has several biochemical functions, for example, contributes_to GPI-anchor transamidase activity,protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by PIGS itself. We selected most functions PIGS had, and list some proteins which have the same functions with PIGS. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
contributes_to GPI-anchor transamidase activity | GPAA1 |
protein binding | KIF5C,DRG2,PITX2,TAX1BP3,NPM1,MYH7,ROCK2,CD14,CNGA1,BAZ1B |
Interacting Protein
PIGS has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PIGS here. Most of them are supplied by our site. Hope this information will be useful for your research of PIGS.
KRTAP10-8;KRT40;NOTCH2NL;GPAA1;DNAJA2;SF3B1;DNAJC8;cona_canen;MYH6;PPM1A
Resources
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References
- Basso, W; Handke, M; et al. Involvement of Toxoplasma gondii in reproductive disorders in Swiss pig farms. PARASITOLOGY INTERNATIONAL 64:157-160(2015).
- Kaser, T; Mair, KH; et al. Natural and inducible Tregs in swine: Helios expression and functional properties. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 49:323-331(2015).