Lipoma Preferred Partner (LPP)

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LIM Domain Containing Preferred Translocation Partner In Lipoma

Lipoma Preferred Partner (LPP)
LPP a member of a subfamily of LIM domain proteins that are characterized by an N-terminal proline rich region and three C-terminal LIM domains. The encoded protein localizes to the cell periphery in focal adhesions and may be involved in cell-cell adhesion and cell motility. This protein also shuttles through the nucleus and may function as a transcriptional co-activator. This gene is located at the junction of certain disease related chromosomal translocations which result in the expression of chimeric proteins that may promote tumor growth. Alternate splicing results in multiple transcript variants.The 612-amino acid open reading frame of LPP showed approximately 85% similarity to zyxin of chicken. Zyxinis a member of the LIM protein family whose members all possess LIM domains.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Lipoma Preferred Partner (LPP) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Lipoma Preferred Partner (LPP) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Lipoma Preferred Partner (LPP) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Lipoma Preferred Partner (LPP) CLIA Kit Customized Service Offer
n/a ELISA Kit for Lipoma Preferred Partner (LPP) ELISA Kit Customized Service Offer

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Lipoma Preferred Partner (LPP) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Lipoma Preferred Partner (LPP) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Lipoma Preferred Partner (LPP) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Lipoma Preferred Partner (LPP) CLIA Kit Customized Service Offer
n/a ELISA Kit for Lipoma Preferred Partner (LPP) ELISA Kit Customized Service Offer

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Lipoma Preferred Partner (LPP) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Lipoma Preferred Partner (LPP) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Lipoma Preferred Partner (LPP) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Lipoma Preferred Partner (LPP) CLIA Kit Customized Service Offer
n/a ELISA Kit for Lipoma Preferred Partner (LPP) ELISA Kit Customized Service Offer
  1. "LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family."Genomics 36:118-129(1996) [PubMed] [Europe PMC] [Abstract]
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  3. "A novel LPP fusion gene indicates the crucial role of truncated LPP proteins in lipomas and pulmonary chondroid hamartomas."Cytogenet. Cell Genet. 95:153-156(2001) [PubMed] [Europe PMC] [Abstract]
  4. "Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in parosteal lipoma."Cancer Genet. Cytogenet. 106:18-23(1998) [PubMed] [Europe PMC] [Abstract]
  5. "An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15)."Genes Chromosomes Cancer 29:363-366(2000) [PubMed] [Europe PMC] [Abstract]
  6. "LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity."Mol. Biol. Cell 11:117-129(2000) [PubMed] [Europe PMC] [Abstract]
  7. "Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23)."Genes Chromosomes Cancer 31:382-389(2001) [PubMed] [Europe PMC] [Abstract]
  8. "The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein."J. Biol. Chem. 278:2157-2168(2003) [PubMed] [Europe PMC] [Abstract]
  9. "The lipoma preferred partner LPP interacts with alpha-actinin."J. Cell Sci. 116:1359-1366(2003) [PubMed] [Europe PMC] [Abstract]
  10. "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract]
  11. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
  12. "The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus."BMC Cell Biol. 6:1-1(2005) [PubMed] [Europe PMC] [Abstract]
  13. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
  15. "A quantitative atlas of mitotic phosphorylation."Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
  17. "Initial characterization of the human central proteome."BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]