OSGEP Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9NPF4 |
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Other Accession | NP_060277.1 |
Clone Names | 91102184 |
Gene ID | 55644 |
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Other Names | Probable tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180}, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, O-sialoglycoprotein endopeptidase {ECO:0000255|HAMAP-Rule:MF_03180}, hOSGEP, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP {ECO:0000255|HAMAP-Rule:MF_03180}, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP {ECO:0000255|HAMAP-Rule:MF_03180}, OSGEP {ECO:0000255|HAMAP-Rule:MF_03180}, GCPL1 |
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 | OSGEP {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000303|PubMed:12039036} |
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Function | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. |
Cellular Location | Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:28805828}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:22912744, ECO:0000269|PubMed:28805828} |
Tissue Location | Widely expressed at low level. Expressed in heart, placenta, liver, kidney, lung, brain, skeletal muscle and pancreas |
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Provided below are standard protocols that you may find useful for product applications.
Background
O-sialoglycoprotein endopeptidases specifically cleave the polypeptide backbone of membrane glycoproteins that contain clusters of O-linked sialoglycans.
References
Naganuma, T., et al. Am. J. Hypertens. 23(2):186-191(2010)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) Seki, Y., et al. Gene 285 (1-2), 101-108 (2002)
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