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GPI8 Antibody (C-term) Blocking Peptide
Synthetic peptide
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- BACKGROUND
| Primary Accession | Q92643 |
|---|---|
| Other Accession | GPI8_HUMAN |
| Clone Names | 3090610 |
| Gene ID | 10026 |
|---|---|
| Other Names | GPI-anchor transamidase, GPI transamidase, 3---, GPI8 homolog, hGPI8, Phosphatidylinositol-glycan biosynthesis class K protein, PIG-K, PIGK, GPI8 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2462b was selected from the C-term region of human GPI8 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PIGK (HGNC:8965) |
|---|---|
| Function | Catalytic subunit of the glycosylphosphatidylinositol-anchor (GPI-anchor) transamidase (GPI-T) complex that catalyzes the formation of the linkage between a proprotein and a GPI-anchor and participates in GPI anchored protein biosynthesis (PubMed:10793132, PubMed:11483512, PubMed:12582175, PubMed:34576938, PubMed:35165458, PubMed:35551457, PubMed:37684232, PubMed:9356492). Recognizes diverse proproteins at a C-terminal signal peptide (CSP) region that lacks consensus sequence and replaces it with a GPI-anchor via a transamidation reaction (PubMed:35165458, PubMed:35551457, PubMed:37684232). Transamidation catalysis reaction follows a two-phase mechanism (PubMed:37684232). In the acyl-enzyme phase, the carbonyl group of the proproteins's omega- site undergoes a nucleophilic attack forming an enzyme-substrate thioester bond (PubMed:37684232). Followed by a general acid catalysis that allows CSP releasing, regenerating the carbonyl, and forming the acyl-enzyme intermediate (PubMed:37684232). In the GPI-anchor attachment phase, the amino group of the GPI-anchor's ethanolamine phosphate, the one on third mannose (EtNP3), mediates a nucleophilic attack on the carbonyl of the acyl-enzyme intermediate, replacing the CSP, allowing GPI-anchor attachment to the omega-residue, therefore forming the product and freeing the enzyme (PubMed:37684232). |
| Cellular Location | Endoplasmic reticulum membrane; Single-pass type I membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
GPI8 is a member of the cysteine protease family C13 that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is a member of the multisubunit enzyme, GPI transamidase and is thought to be its enzymatic component. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins.
References
Ohishi, K., et al., J. Biol. Chem. 278(16):13959-13967 (2003).Vainauskas, S., et al., J. Biol. Chem. 277(34):30535-30542 (2002).Ohishi, K., et al., EMBO J. 20(15):4088-4098 (2001).Meyer, U., et al., Biochemistry 39(12):3461-3471 (2000).Yu, J., et al., Proc. Natl. Acad. Sci. U.S.A. 94(23):12580-12585 (1997).
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