トップ > 製品検索結果一覧 > Code No. D058-3 Anti-Multi Ubiquitin mAb

Code No. D058-3

Anti-Multi Ubiquitin mAb

価格(税別)

¥48,000

在庫

10以上

(2019/12/12 17:00時点)

包装

100 µg/100 µL

Clone FK2 has been reported to recognize K29-, K48-, K63-linked poly ubiquitinylated and mono ubiquitinylated proteins but not free ubiquitin (PMID:18757370, 19237541) .
データ
  • Western Blotting

クローナリティー Monoclonal クローン FK2
アイソタイプ
(免疫動物)
Mouse IgG1 κ
使用法
WB
1-5 µg/mL  
IC*
reported.  (PMID: 12860994 / 15858004 / 16716190
ELISA*
reported.  (PMID: 7588772
IH*
reported.  (PMID: 29097807 / 29282717
免疫原(抗原) a crude poly-ubiquitin-lysozyme
交差性
[Gene ID]

Human, Mouse*(PMID: 15975924/17114435/18083104), Monkey*(PMID: 15858004), Yeast*(PMID: 12724408/15998872), Fruit fly*(PMID: 29456138)

性状 1 mg/mL in PBS/50% glycerol, pH 7.2
保存温度 -20°C 標識 Unlabeled メーカー MBL
背景 Ubiquitin is a polypeptide of 76 amino acid residues, and widely distributed protein in eukaryotic cells. This protein is also highly conserved among eukaryotic cells. Recently several reports showed that intracellular abnormal and short-lived proteins are degradated through an ubiquitin dependent proteolytic pathway. In the ubiquitin dependent pathway, a target protein is tagged with multi-ubiquitin molecules.
関連製品 D058-8 Anti-Multi Ubiquitin mAb-Agarose
D071-3 Anti-Multi Ubiquitin mAb
M162-3 Anti-p62 (SQSTM1) (Human) mAb
PM045 Anti-p62 (SQSTM1) pAb
PM066 Anti-p62 C-terminal pAb
M170-3 Anti-Rubicon (Human) mAb
PD027 Anti-Rubicon (Human) pAb
M113-3 Anti-SUMO-1 mAb
M114-3 Anti-SUMO-2/3 mAb
MK-12-3 Anti-Ubiquitin mAb
MK-11-3 Anti-Ubiquitin mAb
CY-7053 CycLex® Poly-Ubiquitinated Protein ELISA Kit
D058-11 Anti-Multi Ubiquitin mAb-Magnetic Beads
使用文献
使用文献募集中!本製品を使って論文を発表されましたら是非お知らせください。

Western Blotting

  1. Yokosawa N et al. C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein. J Virol. 76, 12683-90 (2002)(PMID:12438594)
  2. Seino H et al. Two ubiquitin-conjugating enzymes, UbcP1/Ubc4 and UbcP4/Ubc11, have distinct functions for ubiquitination of mitotic cyclin. Mol Cell Biol. 23, 3497-3505 (2003)(PMID:12724408)
  3. Inukai N et al. A novel hydrogen peroxide-induced phosphorylation and ubiquitination pathway leading to RNA polymerase II proteolysis. J Biol Chem. 279, 8190-5 (2004)(PMID:14662762)
  4. Yamashita M et al. Ras-ERK MAPK cascade regulates GATA3 stability and Th2 differentiation through ubiquitin-proteasome pathway. J Biol Chem. 280, 29409-19 (2005)(PMID:15975924)
  5. Hwang GW et al. Overexpression of Rad23 confers resistance to methylmercury in saccharomyces cerevisiae via inhibition of the degradation of ubiquitinated proteins. Mol Pharmacol. 68, 1074-8 (2005)(PMID:15998872)
  6. Masuda Y et al. ADRP/adipophilin is degraded through the proteasome-dependent pathway during regression of lipid-storing cells. J Lipid Res. 47, 87-98 (2006)(PMID:16230742)
  7. Hosokawa H et al. Regulation of Th2 cell development by Polycomb group gene bmi-1 through the stabilization of GATA3. J Immunol. 177, 7656-64 (2006)(PMID:17114435)
  8. Komatsu M et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-63 (2007)(PMID:18083104)
  9. Shi W et al. Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation. J Biol Chem. 283, 31608-16 (2008)(PMID:18757370)
  10. Gitcho MA et al. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem. 284, 12384-98 (2009)(PMID:19237541)
  11. Ebina M et al. Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification. PLoS One. 8, e65285 (2013)(PMID:23776465)
  12. Furuya N et al. PARK2/Parkin-mediated mitochondrial clearance contributes to proteasome activation during slow-twitch muscle atrophy via NFE2L1 nuclear translocation. Autophagy 10, 631-41 (2014)(PMID:24451648)
  13. Ogawa M et al. Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome. J Biol Chem. 290, 2137-49 (2015)(PMID:25488668)
  14. Sin Y et al. The C-terminal region and SUMOylation of cockayne syndrome group B protein play critical roles in transcription-coupled nucleotide excision repair. J Biol Chem. 291, 1387-97 (2016)(PMID:26620705)
  15. Takayama Y et al. Dissection of ubiquitinated protein degradation by basal autophagy. FEBS Lett. 591, 1199-1211 (2017)(PMID:28369861)
  16. Okuda K et al. CDKL5 controls postsynaptic localization of GluN2B-containing NMDA receptors in the hippocampus and regulates seizure susceptibility. Neurobiol Dis. 106, 158-170 (2017)(PMID:28688852)
  17. Joachim J et al Centriolar Satellites Control GABARAP Ubiquitination and GABARAP-Mediated Autophagy. Curr Biol. 27, 2123-2136.e7 (2017)(PMID:28712572)
  18. Kim J et al. KLHL7 promotes TUT1 ubiquitination associated with nucleolar integrity: Implications for retinitis pigmentosa. Biochem Biophys Res Commun. 494, 220-226 (2017)(PMID:29032201)
  19. Kang D et al. The InR/Akt/TORC1 Growth-Promoting Signaling Negatively Regulates JAK/STAT Activity and Migratory Cell Fate during Morphogenesis. Dev Cell 44, 524-531.e5. (2018)(PMID:29456138)
  20. Mitsuhashi H et al. Functional domains of the FSHD-associated DUX4 protein. Biol Open 7, bio033977 (2018)(PMID:29618456)
  21. Matsumoto G et al. N-Acyldopamine induces aggresome formation without proteasome inhibition and enhances protein aggregation via p62/SQSTM1 expression. Sci Rep. 8, 9585 (2018)(PMID:29941919)
  22. Jena KK et al. TRIM16 controls assembly and degradation of protein aggregates by modulating the p62‐NRF2 axis and autophagy. EMBO J. 37, e98358 (2018)(PMID:30143514)
  23. Cao Z et al. MDM2 promotes genome instability by ubiquitinating the transcription factor HBP1. Oncogene. 38, 4835-4855 (2019)(PMID:30816344)

Immunocytochemistry

  1. Yokosawa N et al. C-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V protein. J Virol. 76, 12683-90 (2002)(PMID:12438594)
  2. Katoh K et al. The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J Biol Chem. 278, 39104-13 (2003)(PMID:12860994)
  3. Broering TJ et al. Carboxyl-proximal regions of reovirus nonstructural protein muNS necessary and sufficient for forming factory-like inclusions. J Virol. 79, 6194-6206 (2005)(PMID:15858004)
  4. Nakamura M et al. Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes. Genes Cells 11, 593-606 (2006)(PMID:16716190)
  5. Ishioka T et al. Impairment of the ubiquitin-proteasome system by cellular FLIP. Genes Cells 12, 735-44 (2007)(PMID:17573774)
  6. Komatsu M et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-63 (2007)(PMID:18083104)
  7. Shi W et al. Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation. J Biol Chem. 283, 31608-16 (2008)(PMID:18757370)
  8. Gitcho MA et al. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem. 284, 12384-98 (2009)(PMID:19237541)
  9. Choi UY et al. Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies. Exp Mol Med. 47, e159 (2015)(PMID:25882191)
  10. Ohka N et al. SNIPER(TACC3) induces cytoplasmic vacuolization and sensitizes cancer cells to Bortezomib. Cancer Sci. 108, 1032-1041 (2017)(PMID:28192613)
  11. Takayama Y et al. Dissection of ubiquitinated protein degradation by basal autophagy. FEBS Lett. 591, 1199-1211 (2017)(PMID:28369861)
  12. Xie X et al. Deubiquitylases USP5 and USP13 are recruited to and regulate heat-induced stress granules through their deubiquitylating activities. J Cell Sci. 131, jcs210856 (2018)(PMID:29567855)

Immunohistochemistry

  1. Tsuji H et al. TDP-43 accelerates age-dependent degeneration of interneurons. Sci Rep. 7, 14972 (2017)(PMID:29097807)
  2. Watanabe S et al. Intracerebroventricular administration of Cystatin C ameliorates disease in SOD1-linked amyotrophic lateral sclerosis mice. J Neurochem. 145, 80-89 (2018)(PMID:29282717)
製品
カテゴリー
分野
オートファジー
ユビキチンプロテアソーム系
この製品に関するお問い合わせをする

※在庫につきましては2019年12月12日 17時00分時点における在庫数を表示してあります。
※価格の赤色表示につきましては、キャンペーン価格の表示となっております。
※このサイトからは直接注文はできません。ご注意ください。
※使用法の表記について:
WB: Western Blotting, IH: Immunohistochemistry, IC: Immunocytochemistry, IP: Immunoprecipitation,
FCM: Flow Cytometry NT: Neutralization, IF: Immunofluorescence, RIP: RNP Immunoprecipitation,
ChIP: Chromatin Immunoprecipitation, CoIP: Co-Immunoprecipitation
DB: Dot Blotting, NB: Northern Blotting, RNA FISH: RNA Fluorescence in situ hybridization
※使用法・交差性の表記について:
*: 論文で報告されております(MBLでは未確認)。詳しくはデータシートをご覧ください。
**: 導入元からの情報です(MBLでは評価中もしくは未確認)。
※保存温度の表記について: RT: 室温
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