Antibody data
- Antibody Data
- Antigen structure
- References [6]
- Comments [0]
- Validations [0]
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- Product number
- ABIN351325 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN351325, RRID:AB_10788549
- Product name
- anti-Vacuolar Protein Sorting 29 Homolog (S. Cerevisiae) (VPS29) (C-Term) antibody
- Antibody type
- Polyclonal
- Antigen
- A synthetic peptide from the c-terminal of mouse VPS29 conjugated to an immunogenic carrier protein was used as the antigen. The antigen is homologous in rat, human, chicken, zebra fish and xenopus.
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- C-Term
- Vial size
- 100 μL
- Storage
- Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability.
- Handling
- Avoid freeze and thaw cycles.
Submitted references Functional architecture of the retromer cargo-recognition complex.
The transcriptional landscape of the mammalian genome.
Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly.
The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor.
Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.
Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes.
Hierro A, Rojas AL, Rojas R, Murthy N, Effantin G, Kajava AV, Steven AC, Bonifacino JS, Hurley JH
Nature 2007 Oct 25;449(7165):1063-7
Nature 2007 Oct 25;449(7165):1063-7
The transcriptional landscape of the mammalian genome.
Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schönbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y, FANTOM Consortium, RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
Science (New York, N.Y.) 2005 Sep 2;309(5740):1559-63
Science (New York, N.Y.) 2005 Sep 2;309(5740):1559-63
Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly.
Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ
Nature structural & molecular biology 2005 Jul;12(7):594-602
Nature structural & molecular biology 2005 Jul;12(7):594-602
The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor.
Vergés M, Luton F, Gruber C, Tiemann F, Reinders LG, Huang L, Burlingame AL, Haft CR, Mostov KE
Nature cell biology 2004 Aug;6(8):763-9
Nature cell biology 2004 Aug;6(8):763-9
Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A
Genome research 2001 Mar;11(3):422-35
Genome research 2001 Mar;11(3):422-35
Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes.
Haft CR, de la Luz Sierra M, Bafford R, Lesniak MA, Barr VA, Taylor SI
Molecular biology of the cell 2000 Dec;11(12):4105-16
Molecular biology of the cell 2000 Dec;11(12):4105-16
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