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OP97

Sigma-Aldrich

Anti-mTOR/FRAP (Ab-2) Mouse mAb (22C2)

liquid, clone 22C2, Calbiochem®

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About This Item

UNSPSC Code:
12352203

biological source

mouse

Quality Level

100

antibody form

purified antibody

antibody product type

primary antibodies

clone

22C2, monoclonal

form

liquid

contains

≤0.1% sodium azide as preservative

species reactivity

human

manufacturer/tradename

Calbiochem®

storage condition

do not freeze

isotype

IgG1

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

human ... MTOR(2475)

General description

Purified mouse monoclonal antibody generated by immunizing mice with the specified immunogen and fusing splenocytes with SpAG8 mouse myeloma cells. Recognizes the ~290 kDa mTOR/FRAP protein.
Recognizes the ~290 kDa mTOR protein in HEK293 and Jurkat cells.
This Anti-mTOR/FRAP (Ab-2) Mouse mAb (22C2) is validated for use in Immunoblotting, Immunoprecipitation for the detection of mTOR/FRAP (Ab-2).

Immunogen

Human
a synthetic peptide corresponding to amino acids 230-240 of human TOR

Application


Immunoblotting (1.7 g/ml, see application references)
Immunoprecipitation (1-10 g/ml, see application references)

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Physical form

In 50 mM sodium phosphate buffer, 0.2% gelatin.

Analysis Note

Positive Control
Jurkat or HeLa cells

Other Notes

Kimura N et al. 2003. Genes Cells8, 65.
Sekulic A et al. 2000. Cancer Res.60, 3504.
Hosoi, H. 1999. Cancer Res.59, 886.
Alarcon, C.M., et al. 1996. Genes Dev.10, 279.
Freeman, K., and Livi, G.P. 1996. Gene172, 143.
Hosoi, H., et al. 1996. AACR 87th Ann. Mtg. Abstract 3445.
Cardenas, M.E., and Heitman, J. 1995. EMBO J.14, 5892.
Lorenz, M.C., and Heitman, J. 1995. J. Biol. Chem.270, 27531.
Sabatini, D.M., et al. 1995. J. Biol. Chem.270, 20875.
Zheng, X.F., et al. 1995. Cell82, 121.
Brown, E.J., et al. 1994. Nature369, 756.
Sabatini, D.M., et al. 1994. Cell78, 35.
Stan, R., et al. 1994. J. Biol. Chem.269, 32027.
Kunz, J., et al. 1993. Cell73, 585.
Heitman, J., et al. 1991. Science253, 905.
The immunogen sequence is 100% conserved in mouse and rat, but cross-reactivity has not been tested. Antibody should be titrated for optimal results in individual systems.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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M C Lorenz et al.
The Journal of biological chemistry, 270(46), 27531-27537 (1995-11-17)
The antifungal, immunosuppressive compound rapamycin arrests the cell cycle in G1 in both yeast cells and T-lymphocytes. Previous genetic studies in yeast identified mutations in three genes, FPR1 (FKBP12), TOR1, and TOR2, which confer rapamycin resistance, and genetic findings implicated
R Stan et al.
The Journal of biological chemistry, 269(51), 32027-32030 (1994-12-23)
The yeast TOR1 and TOR2 proteins were previously discovered as putative targets of the immunosuppressive drug rapamycin. Although their cellular function is unknown, they are predicted to be at least 215 kDa in size and possess a C-terminal phosphatidylinositol (PI)
J Kunz et al.
Cell, 73(3), 585-596 (1993-05-07)
The yeast TOR2 gene encodes an essential 282 kd phosphatidylinositol (PI) 3-kinase homolog. TOR2 is related to the catalytic subunit of bovine PI 3-kinase and to yeast VPS34, a vacuolar sorting protein also shown to have PI 3-kinase activity. The
C M Alarcon et al.
Genes & development, 10(3), 279-288 (1996-02-01)
In complex with the prolyl isomerase FKBP12, the natural product rapamycin blocks signal transduction in organisms as diverse as yeast and man. The yeast targets of FKBP12-rapamycin, TOR1 and TOR2, are large proteins with homology to lipid and protein kinases.
K Freeman et al.
Gene, 172(1), 143-147 (1996-06-12)
The TOR genes were first identified in Saccharomyces cerevisiae by the isolation of mutants which exhibit dominant resistance to the immunosuppressive and antifungal drug rapamycin (Rm). The originally characterized Rm-resistant (RmR) TOR1-1 and TOR2-1 alleles contain an Arg in place
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