Anti-Runx2 (Cbfa1) mAb

  • Applications
    • ELISA
    • ICC
    • IHC
    • IP
    • WB
  • Target Runx2/Cbfa1/AML-3
  • Host Species Mouse
  • Species Reactivities Human, Mouse
  • Code # D130-3
  • Size 100 μg
  • Price
    $328.61
Specifications

Alternative Names

PEBP2αA

Background

​Runx2, also known as Cbfa1 or PEBP2αA, is an essential transcription factor of skeletal tissues that is involved in the regulation of osteoblast differentiation and bone formation. Runx2-null mice have neither bone tissue nor osteoblasts. FGF receptor signaling, TGF-β, and BMP all activate transcription of Runx2, resulting in inhibition of myogenesis and myogenic differentiation. BMP-induced Runx2 cooperates with BMP-activated Smads to induce osteogenesis. Runx2 has also been shown to play a role in the regulation of chondrocyte hypertrophy and tooth eruption.
  • Antibody Type:
    Monoclonal
  • Application:
    ELISA, ICC, IHC, IP, WB
  • Clone Number:
    8G5
  • Concentration:
    1 mg/mL
  • Conjugate:
    Unlabeled
  • Description:
    Monoclonal antibody of 100 μg targeting Runx2/Cbfa1/AML-3 for ICC, IPP, WB, ELISA, IHC.
  • Formulation:
    100 μg IgG in 100 μl volume of PBS containing 50% glycerol, pH 7.2. No preservative iscontained.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Gene ID (Rat):
  • Host Species:
    Mouse
  • Immunogen:
    Recombinant Runx2
  • Isotype:
    IgG2b
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts with human Runx2/Cbfa1 (66kDa) and mouse Runx2/Cbfa1 (55kDa) by Western blotting.
  • Research Area:
    Cancer
  • Short Description:
    Runx2/Cbfa1/AML-3 Monoclonal Antibody.
  • Size:
    100 μg
  • Species Reactivity:
    Human, Mouse
  • Storage Temperature:
    -20°C
  • Target:
    Runx2/Cbfa1/AML-3
Citations
  1. Ali SA et al. A RUNX2-HDAC1 co-repressor complex regulates rRNA gene expression by modulating UBF acetylation. J Cell Sci. 125, 2732-9 (2012),
  2. Beier EE et al. Heavy metal lead exposure, osteoporotic-like phenotype in an animal model, and depression of Wnt signaling. Environ Health Perspect. 121, 97-104 (2013),
  3. Fulzele K et al. Insulin receptor signaling in osteoblasts regulates postnatal bone acquisition and body composition. Cell 142, 309-19 (2010),
  4. Hirata A et al. Localization of runx2, osterix, and osteopontin in tooth root formation in rat molars. J Histochem Cytochem. 57, 397-403 (2009),
  5. Hosoya A et al. Two distinct processes of bone-like tissue formation by dental pulp cells after tooth transplantation. J Histochem Cytochem. 60, 861-73 (2012),
  6. Kaneki H et al. Tumor necrosis factor promotes Runx2 degradation through up-regulation of Smurf1 and Smurf2 in osteoblasts. J Biol Chem. 281, 4326-33 (2006),
  7. Kugimiya F et al. GSK-3beta controls osteogenesis through regulating Runx2 activity. PLoS One. 2, e837 (2007),
  8. Lau QC et al. RUNX3 is frequently inactivated by dual mechanisms of protein mislocalization and promoter hypermethylation in breast cancer. Cancer Res. 66, 6512-20 (2006),
  9. Ohba S et al. Identification of a potent combination of osteogenic genes for bone regeneration using embryonic stem (ES) cell-based sensor. FASEB J. 21, 1777-87 (2007),
  10. Standal T et al. HGF inhibits BMP-induced osteoblastogenesis: possible implications for the bone disease of multiple myeloma. Blood. 109, 3024-30 (2007),
  11. Tandon M et al. Runx2 activates PI3K/Akt signaling via mTORC2 regulation in invasive breast cancer cells. Breast Cancer Res. 16, R16 (2014),
  12. Taniguchi N et al. Expression patterns and function of chromatin protein HMGB2 during mesenchymal stem cell differentiation. J Biol Chem. 286, 41489-98 (2011),
  13. Tominaga H et al. CCAAT/enhancer-binding protein beta promotes osteoblast differentiation by enhancing Runx2 activity with ATF4. Mol Biol Cell. 19, 5373-86 (2008),
  14. Underwood KF et al. Regulation of RUNX2 transcription factor-DNA interactions and cell proliferation by vitamin D3 (cholecalciferol) prohormone activity. J Bone Miner Res. 27, 913-25 (2012),
  15. Wang Q et al. Bone morphogenetic protein 2 activates Smad6 gene transcription through bone-specific transcription factor Runx2. J Biol Chem. 282, 10742-8 (2007),
  16. Wee HJ et al. Serine phosphorylation of RUNX2 with novel potential functions as negative regulatory mechanisms. EMBO Rep. 3, 967-74 (2002),
  17. Zhang YW et al. A RUNX2/PEBP2alpha A/CBFA1 mutation displaying impaired transactivation and Smad interaction in cleidocranial dysplasia. PNAS 97, 10549-54. (2000)
References
  1. Beier, E. E., et al., Environ.Health Perspect. 121, 97-104(2013) [IHC]
  2. Underwood, K. F., et al., J.Bone Miner. Res. 27, 913-925 (2012) [WB, ELISA]
  3. Hosoya, A., et al., J.Histochem.Cytochem. 60, 861-73(2012) [IHC]
  4. Ali, S. A., et al., J. Cell Sci. 125, 2732-2739 (2012) [IC]
  5. Fulzele, K., et al., Cell 142, 309-319 (2011) [ChIP]
  6. Hirata,A., et al., J.Histochem.Cytochem. 57, 397-403 (2009)[IHC]
  7. Tominaga, H., et al., Mol. Biol. Cell 19, 5373-5386 (2008) [WB]
  8. Ohba, S., et al., FASEB J. 21, 1777-1787 (2007) [WB, IP, ChIP]
  9. Wang, Q., et al., J.Biol.Chem. 282, 10742-10748 (2007)[ChIP]
  10. Lau, Q. C., et al., Cancer Res. 66, 6512-6520 (2006) [WB, IC]
  11. Kaneki, H., et al., J. Biol. Chem. 281, 4326-4333 (2006) [WB]
  12. Wee, H. J., et al., EMBO Rep. 3, 967-974 (2002) [WB, IP]
  13. Zhang, Y. W., et al., PNAS 97, 10549-10554 (2000) [WB]