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STT3A Antibody (Center)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - STT3A Antibody (Center) AP22179c
    Anti-STT3A Antibody (Center) at 1:2000 dilution + K562 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 81 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 1 - STT3A Antibody (Center) AP22179c
    Anti-STT3A Antibody (Center) at 1:2000 dilution + human placenta lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 81 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
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, E
Primary Accession P46977
Other Accession Q2KJI2, P46978, Q5RCE2
Reactivity Human
Predicted Bovine, Mouse
Host Rabbit
Clonality polyclonal
Isotype Rabbit Ig
Calculated MW 80530 Da
Additional info
Gene ID 3703
Other Names Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A, Oligosaccharyl transferase subunit STT3A, STT3-A, 2.4.99.18, B5, Integral membrane protein 1, Transmembrane protein TMC, STT3A, ITM1, TMC
Target/Specificity This STT3A antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 476-507 amino acids from the Central region of human STT3A.
Dilution WB~~1:2000
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.
PrecautionsSTT3A Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name STT3A
Synonyms ITM1, TMC
Function Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.
Cellular Location Endoplasmic reticulum membrane; Multi-pass membrane protein
Tissue Location Expressed at high levels in placenta, liver, muscle and pancreas, and at very low levels in brain, lung and kidney. Expressed in skin fibroblasts (at protein level)

BACKGROUND

Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.

REFERENCES

Hong G.,et al.Genomics 31:295-300(1996).
Lissy N.A.,et al.Biochim. Biophys. Acta 1306:137-141(1996).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Taylor T.D.,et al.Nature 440:497-500(2006).

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