推荐产品
生物源
mouse
品質等級
抗體表格
ascites fluid
抗體產品種類
primary antibodies
無性繁殖
monoclonal
物種活性
E. coli
製造商／商標名
Chemicon®
技術
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
同型
IgG2a
UniProt登錄號
運輸包裝
dry ice
目標翻譯後修改
unmodified
基因資訊
Escherichia coli ... PhoA(945041)
特異性
Alkaline phosphatase (AP). MAB1012 has a high affinity and recognizes an AP determinant resistant to denaturation by SDS-PAGE. It is therefore ideally suited for sensitive and specific detection of AP fusion proteins by Western blot analysis of E. coli transformants expressing fusion products.
免疫原
Epitope: E. coli, bacterial only
F201C1B
應用
Anti-Alkaline Phosphatase Antibody, E. coli, bacterial only detects level of Alkaline Phosphatase & has been published & validated for use in IP, WB & IC.
Western blot at 1:5,000. 42-45kDa on SDS-PAGE,reducing gels for natural E. coli alkaline phosphatase monomer. Alkaline phosphatase fusion proteins will vary depending upon the target fusion protein.
Immunocytochemistry: reacts with E.coli. AP fusion protein targets in acetone fixed cell preparations. 1:4000, other fixatives or conditions untested.
ASSAY:
Preparation of E. coli TnphoA transformants: E. coli strain CC118 was transformed with plasmid pGEM-3Z containing TnphoA insertional mutations in the p101 gene of Mycoplasma hyorhinis, which encodes a protein with a typical N-terminal prokaryotic single peptide (Yogev et al. 1991).
Identification of fusion protein with MAB1012 transformants: Transformants are grown in 2XYT medium to OD600=0.6. Cells were centrifuged 3 minutes at 10,000 x g, suspended in SDS-PAGE sample buffer, heated at 100°C for 5 minutes, frozen and thawed and centrifuged as above at room temperature to remove insoluble material. The sample is applied at 9% to a SDS-PAGE gel, and Western immunoblot is performed as described (Yogev et al. 1991).
Immunoprecipitation: 5μL of antibody per 500μL of lysate in RIPA or 0.5% triton X-100 solutions.
Optimal working dilutions must be determined by end user.
Immunocytochemistry: reacts with E.coli. AP fusion protein targets in acetone fixed cell preparations. 1:4000, other fixatives or conditions untested.
ASSAY:
Preparation of E. coli TnphoA transformants: E. coli strain CC118 was transformed with plasmid pGEM-3Z containing TnphoA insertional mutations in the p101 gene of Mycoplasma hyorhinis, which encodes a protein with a typical N-terminal prokaryotic single peptide (Yogev et al. 1991).
Identification of fusion protein with MAB1012 transformants: Transformants are grown in 2XYT medium to OD600=0.6. Cells were centrifuged 3 minutes at 10,000 x g, suspended in SDS-PAGE sample buffer, heated at 100°C for 5 minutes, frozen and thawed and centrifuged as above at room temperature to remove insoluble material. The sample is applied at 9% to a SDS-PAGE gel, and Western immunoblot is performed as described (Yogev et al. 1991).
Immunoprecipitation: 5μL of antibody per 500μL of lysate in RIPA or 0.5% triton X-100 solutions.
Optimal working dilutions must be determined by end user.
外觀
Ascites. Contains no preservative.
法律資訊
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
Sequence and TnphoA analysis of a Mycoplasma hyorhinis protein with membrane export function.
Yogev, D, et al.
Journal of Bacteriology, 173, 2035-2044 (1991)
A genetic approach to analyzing membrane protein topology.
Manoil, C and Beckwith, J
Science (New York, N.Y.), 233, 1403-1408 (1986)
Both the stroma and thylakoid lumen of tobacco chloroplasts are competent for the formation of disulphide bonds in recombinant proteins.
Julia Bally,Eric Paget,Michel Droux,Claudette Job,Dominique Job,Manuel Dubald
Plant Biotechnology Journal null
Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion.
Hoffman, C S and Wright, A
Proceedings of the National Academy of Sciences of the USA, 82, 5107-5111 (1985)
TnphoA: a transposon probe for protein export signals.
Manoil, C and Beckwith, J
Proceedings of the National Academy of Sciences of the USA, 82, 8129-8133 (1985)
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