Cell Signaling Technology

Product Pathways - Protein Stability

USP9X (D4Y7W) Rabbit mAb #14898

Deubiquitylating Enzymes   DUBs   USP9   USP9X  

No. Size Price
14898S 100 µl ( 10 western blots ) ¥3,100.00 现货查询 购买询价
14898 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 270 Rabbit IgG
IP 1:50
IHC-P 1:100
IF-IC 1:400

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry),

Homology

Species predicted to react based on 100% sequence homology: Bovine, Dog, Horse,

Specificity / Sensitivity

USP9X (D4Y7W) Rabbit mAb recognizes endogenous levels of total USP9X protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn1272 of human USP9X protein.

IF-IC

IF-IC

Confocal immunofluorescent analysis of 293T (left, positive) and LOX-IMVI (right, negative) cells using USP9X (D4Y7W) Rabbit mAb (green). Actin filaments were labeled with DyLight™ 554 Phalloidin #13054 (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded PC-3 (left, positive) and LOX-IMVI (right, negative) cell pellets using USP9X (D4Y7W) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human prostate carcinoma using USP9X (D4Y7W) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma using USP9X (D4Y7W) Rabbit mAb in the presence of control peptide (left) or antigen-specific peptide (right).

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using USP9X (D4Y7W) Rabbit mAb (upper) and GAPDH (D16H11) XP® Rabbit mAb #5174 (lower). LOX-IMVI cells are deficient in USP9X protein expression (13).

IP

IP

Immunoprecipitation of USP9X from 293T cell extracts using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or USP9X (D4Y7W) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using USP9X (D4Y7W) Rabbit mAb.

Background

Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) respectively (1,2). DUBs are categorized into five subfamilies-USP, UCH, OTU, MJD, and JAMM. Ubiquitin-specific protease 9, X-linked (USP9X) possesses a well-conserved catalytic domain with cysteine peptidase activity, which allows for cleavage of ubiquitin and polyubiquitin conjugates. USP9X is the mammalian homolog of the Drosophila fat-facets (faf) gene, which is essential for normal eye development and viability of the early fly embryo (3,4). While USP9X expression is also critical for normal mammalian development (5-7), many of its substrates are only beginning to be elucidated. There is mounting evidence that USP9X functions in the formation of epithelial cell-cell contacts through deubiquitination-dependent stabilization of molecules involved in maintaining the integrity of both adherens and tight junctions. Indeed, USP9X has been found to associate with AF-6, the β-catenin-E-cadherin complex, and EFA6 (8-11). Research studies have also demonstrated that USP9X is an integral component of the TGF-β/BMP signaling cascade by opposing TRIM33-mediated monoubiquitination of SMAD4 (12). USP9X is overexpressed in a variety of human cancers and contributes to enhanced cell survival, in part, through its ability to deubiquitinate and stabilize the Mcl-1 oncoprotein (13). There is some evidence, however, that suggests the role of USP9X in tumorigenesis is context dependent. Research studies have implicated USP9X in a tumor suppressor role during the early stages of pancreatic ductal adenocarcinoma (PDAC) and in an oncogenic role during advanced stages of PDAC (14,15).

  1. Nijman, S.M. et al. (2005) Cell 123, 773-86.
  2. Nalepa, G. et al. (2006) Nat Rev Drug Discov 5, 596-613.
  3. Huang, Y. et al. (1995) Science 270, 1828-31.
  4. Huang, Y. and Fischer-Vize, J.A. (1996) Development 122, 3207-16.
  5. Pantaleon, M. et al. (2001) Mech Dev 109, 151-60.
  6. Noma, T. et al. (2002) Mech Dev 119 Suppl 1, S91-5.
  7. Xu, J. et al. (2005) J Neurosci Res 80, 47-55.
  8. Taya, S. et al. (1998) J Cell Biol 142, 1053-62.
  9. Taya, S. et al. (1999) Genes Cells 4, 757-67.
  10. Murray, R.Z. et al. (2004) Mol Biol Cell 15, 1591-9.
  11. Théard, D. et al. (2010) EMBO J 29, 1499-509.
  12. Dupont, S. et al. (2009) Cell 136, 123-35.
  13. Schwickart, M. et al. (2010) Nature 463, 103-7.
  14. Pérez-Mancera, P.A. et al. (2012) Nature 486, 266-70.
  15. Cox, J.L. et al. (2014) Cancer Biol Ther 15, 1042-52.

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