p190-A RhoGAP Antibody

p190-A RhoGAP Antibody

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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年12月09日
  • W
  • Rabbit
  • H,M,R,Hm
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    • 详细信息
    • 技术资料
    • 抗体英文名

      p190-A RhoGAP Antibody

    • 抗原

      synthetic peptide corresponding to central residues of human p190-A RhoGAP

    • 应用范围

      W

    • 宿主

      Rabbit

    • 供应商

      CST

    • 库存

      大量

    • 保质期

      详见说明书

    • 级别

      详见MSDS文件

    • 适应物种

      H,M,R,Hm

    • 是否单克隆

      2

    • 保存条件

      -20°c

    • 规格

      100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting
    Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W H M R Hm Endogenous 190 kDa Rabbit
    Protocols
    Specificity / Sensitivity

    p190-A RhoGAP Antibody detects endogenous levels of total p190-A RhoGAP protein (GRLF1).

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to central residues of human p190-A RhoGAP. Antibodies are purified by peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from various cell types using p190-A RhoGAP Antibody.

    Background

    The Rho family of small GTPases, including Rho, Rac and Cdc42, are key regulators of diverse biological processes such as cytoskeletal organization, cell growth and differentiation, transcriptional regulation, and cell adhesion/motility (1,2). The activities of these proteins are controlled by GTP binding such that in the GTP-bound state they are active, and in the GDP-bound state they become inactive. Three classes of regulatory proteins control the activity of the GTPases by balancing the levels of GTP/GDP binding: the guanine nucleotide exchange factors (GEFs), which promote the active state by facilitating the exchange of GDP for GTP; the guanine nucleotide dissociation inhibitors (GDIs), which sequester the GDP-bound forms and may regulate their intracellular localization; and the GTPase activating proteins (GAPs), which increase GTP hydrolysis to promote the inactive state. The p190 RhoGAP family consists of two related proteins, p190-A and p190-B, which are both widely expressed and contain an amino-terminal GTPase domain and a carboxy-terminal RhoGAP catalytic domain. Mice lacking p190-B RhoGAP show excessive Rho activation and a reduction in activation of the transcription factor CREB (3). Phenotypes of these mice are similar to those of CREB knockouts, with reduced cell size, as well as defects in thymus and neural development (3). Cells deficient in p190-B also display defective adipogenesis, suggesting this pathway is critical for the "adipogenesis-myogenesis switch." (4). There is increasing evidence that p190 undergoes tyrosine phosphorylation, which activates its GAP domain (4-6). Levels of tyrosine phosphorylation are enhanced by Src overexpression (5,6). IGF-1 treatment downregulates Rho through phosphorylation and activation of p190-B RhoGAP, thereby enhancing IGF signaling implicated in adipogenesis (4).

    p190-A has been characterized as a tumor suppressor based on its ability to reverse v-Ha-Ras-induced malignancy in cultured cells (7). Loss or rearrangement of the chromosomal region containing the gene for p190-A has been implicated in the development of some human tumors (8). p190-A can also bind the mitogen-inducible transcription factor TFII-I sequestering it in the cytoplasm and inhibiting its activity. Phosphorylation of p190-A at Tyr308 reduces its affinity for TFII-I, relieving the inhibition (9). p190-A can also inhibit growth factor-induced gliomas in mice (10) and affect cleavage furrow formation and cytokinesis in cultured cells (11).

    1. Peck, J. et al. (2002) FEBS Lett. 528, 27-34.
    2. Moon, S.Y. and Zheng, Y. (2003) Trends Cell Biol. 13, 13-22.
    3. Sordella, R. et al. (2002) Dev. Cell 2, 553-565.
    4. Sordella, R. et al. (2003) Cell 113, 147-158.
    5. Chang, J. H. et al. (1995) J. Cell. Biol. 130, 355-368.
    6. Roof, R. W. et al. (1998) Mol. Cell. Biol. 18, 7052-7063.
    7. Wang, Z. et al. (1996) Cell Growth Differ. 7, 123-133.
    8. Tikoo, A. et al. (2000) Gene 257, 23-31.
    9. Jiang, W. et al. (2005) Mol. Cell 17, 23-35.
    10. Wolf, R.M. et al. (2003) Genes Dev. 17, 476-487.
    11. Su, L. et al. (2003) J. Cell Biol. 163, 571-582.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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