生物源
mouse
品質等級
抗體表格
purified antibody
抗體產品種類
primary antibodies
無性繁殖
22C2, monoclonal
形狀
liquid
包含
≤0.1% sodium azide as preservative
物種活性
human
製造商/商標名
Calbiochem®
儲存條件
do not freeze
同型
IgG1
運輸包裝
wet ice
儲存溫度
2-8°C
目標翻譯後修改
unmodified
基因資訊
human ... MTOR(2475)
一般說明
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).
免疫原
Human
a synthetic peptide corresponding to amino acids 230-240 of human TOR
應用
Immunoblotting (1.7 g/ml, see application references)
Immunoprecipitation (1-10 g/ml, see application references)
包裝
Please refer to vial label for lot-specific concentration.
警告
Toxicity: Standard Handling (A)
外觀
In 50 mM sodium phosphate buffer, 0.2% gelatin.
分析報告
Positive Control
Jurkat or HeLa cells
Jurkat or HeLa cells
其他說明
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.
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.
法律資訊
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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儲存類別代碼
11 - Combustible Solids
水污染物質分類(WGK)
WGK 1
閃點(°F)
Not applicable
閃點(°C)
Not applicable
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
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)
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
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.
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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