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GPI8 Antibody (N-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - GPI8 Antibody (N-term) AP2462a
    The anti-GPI8 Pab (Cat. #AP2462a) is used in Western blot to detect GPI8 in 293 cell lysate.
  • 14 - GPI8 Antibody (N-term) AP2462a
    Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, E
Primary Accession Q92643
Other Accession Q4KRV1, Q9CXY9, Q3MHZ7
Reactivity Human
Predicted Bovine, Mouse, Pig
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 45252 Da
Antigen Region 37-68 aa
Additional Information
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 This GPI8 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 37-68 amino acids from the N-terminal region of human GPI8.
Dilution WB~~1:1000
IHC-P~~1:100~500
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsGPI8 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
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
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

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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