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PTEN antibody RabMAb®

Cat.#: 3615-1
Abcam ID: ab133254

Rabbit Monoclonal Antibody


Clone ID: EPR4408
Swiss Prot: P60484
Mol Weight: 54kDa
Size: 100ul
Price: $295

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Bulk and Custom formulation available Email request


Description

PTEN is a protein tyrosine phosphatase that acts as a tumor suppressor, lipid phosphatase that dephosphorylates the D3 position of phosphatidylinositol 3,4,5-trisphosphate, and antagonist of the PI3k/AKT signaling pathway (1-3). PTEN structural domains includes an N-terminal phosphatase domain, a lipid binding C2 domain and a 50-amino acid C-terminal tail that contains a PD binding sequence (5). Phosphorylation of the tail of the protein will suppress its activity and modify its conformation from an open to closed form (5). Mutations in PTEN have been linked to glioblastoma, melanoma and prostate cancer.

Recommended Applications

WB, FC

Applications and Recommended Dilution Factors

WB: 1:1,000-10,000
FC: 1:10 - 100

Species Reactivity *

Human, Mouse, Rat

*Species cross-reactivity is based on WB analysis


Products Data

Western blot analysis on (A) MCF-7, (B) HeLa, and (C) 293T cell lysates using anti-PTEN RabMAb (cat. #3615-1).Flow cytometric analysis of permeabilized MCF-7 cells using anti-PTEN RabMAb (red) (catalog # 3615-1) or a rabbit IgG (negative) (green).

Specificity

A full length recombinant human PTEN was used as an immunogen.

Storage Condition and Buffer

Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.

Alternative Names

PTEN antibody, 10q23del antibody, BZS antibody, DEC antibody, GLM2 antibody, MHAM antibody, MMAC1 antibody, PTEN1 antibody, TEP1 antibody, Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN antibody, Mutated in multiple advanced cancers 1 antibody, Phosphatase and tensin homolog antibody

Description References

1. Vazquez, F., and Sellers, W. R. (2000) Biochim. Biophys. Acta 1470, M21-M35
2. Maehama, T., and Dixon, J. E. (1998) J. Biol. Chem. 273, 13375-13378
3. Maehama, T., Taylor, G. S., and Dixon, J. E. (2001) Annu. Rev. Biochem. 70, 247-279
4. Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M. & Cantley, L. C. (1997) Science 275, 73-77
5. Francisca Vazquez, Steven R. Grossman, Yuki Takahashi, Mihail V. Rokas, Noriaki Nakamura, and William R. Sellers, J. Biol. Chem., Vol. 276, Issue 52, 48627-48630, December 28, 2001

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