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- Product number
- ABIN951616 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Component of Oligomeric Golgi Complex 3 (COG3) (AA 673-703), (C-Term) antibody
- Antibody type
- Polyclonal
- Description
- Affinity chromatography on Protein A
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- C-Term, AA 673-703
- Vial size
- 0.4 mL
- Storage
- Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
- Handling
- Avoid repeated freezing and thawing.
Submitted references Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.
COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation.
The binary interacting network of the conserved oligomeric Golgi tethering complex.
The DNA sequence and analysis of human chromosome 13.
Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.
Laufman O, Kedan A, Hong W, Lev S
The EMBO journal 2009 Jul 22;28(14):2006-17
The EMBO journal 2009 Jul 22;28(14):2006-17
COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation.
Shestakova A, Zolov S, Lupashin V
Traffic (Copenhagen, Denmark) 2006 Feb;7(2):191-204
Traffic (Copenhagen, Denmark) 2006 Feb;7(2):191-204
The binary interacting network of the conserved oligomeric Golgi tethering complex.
Loh E, Hong W
The Journal of biological chemistry 2004 Jun 4;279(23):24640-8
The Journal of biological chemistry 2004 Jun 4;279(23):24640-8
The DNA sequence and analysis of human chromosome 13.
Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT
Nature 2004 Apr 1;428(6982):522-8
Nature 2004 Apr 1;428(6982):522-8
Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J
Nature biotechnology 2003 May;21(5):566-9
Nature biotechnology 2003 May;21(5):566-9
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