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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Use Anti-p53 Antibody, clone PAb421 (Mouse Monoclonal Antibody) validated in WB, IP, IHC to detect p53 also known as Cellular tumor antigen p53, Tumor suppressor p53.
More>>Use Anti-p53 Antibody, clone PAb421 (Mouse Monoclonal Antibody) validated in WB, IP, IHC to detect p53 also known as Cellular tumor antigen p53, Tumor suppressor p53. Less<<
Anti-p53 Antibody, clone PAb421: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
p53 was discovered in 1979 as a cellular protein associating with the transforming protein of SV40 tumor virus. Since then, many different biochemical functions have been attributed to the 53 kDa phosphoprotein. Experimental evidence has suggested that p53 acts as a negative regulator of cell growth in normal cells). Thus, the inactivation or mutation of p53 may be an essential step in the development of malignancy. Wild-type p53 levels in normal cells and tissues were found to be very low. Mutant p53 polypeptide, however, is often found to be present at high concentrations in mammalian tumors and tumor cell lines. For example, in an immuno-histochemistry study 40% of human breast cancer showed elevated levels of mutant p53 in the cell nucleus. Mutations of the p53 protein have some characteristic features: Most of them are missense point mutations giving rise to an altered protein function. Also, many, but not all, mutant p53 proteins exhibit a common mutant structure, which can be recognized by monoclonal antibodies specific for p53 in the mutant conformation.
References
Product Information
Format
Purified
Control
Mouse brain tissue lysate
Presentation
Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Use Anti-p53 Antibody, clone PAb421 (Mouse Monoclonal Antibody) validated in WB, IP, IHC to detect p53 also known as Cellular tumor antigen p53, Tumor suppressor p53.
Key Applications
Western Blotting
Immunoprecipitation
Immunohistochemistry
Application Notes
Immunoprecipitation Analysis: A representative lot from independent laboratory immunoprecipitated p53 in IP (Lehman, T. A., et al. (1991). Cancer Res. 51(15):4090-4096.; Harlow, E., et al. (1981). J Virol. 39(3):861-869.)
Immunohistochemistry Analysis: A representative lot from an independent laboratory detected p53 in human breast cancer tissue (Davidoff, A. M., et al. (1992). Proc Natl Acad Sci USA. 89(8):3439-3442.).
Biological Information
Immunogen
Partially purified mouse p53
Epitope
Amino acids 376-378 in human p53
Clone
PAb421
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
This antibody recognizes amino acids 376-378 of human p53.
Isotype
IgG2aκ
Species Reactivity
Mouse
Species Reactivity Note
Demonstrated to react with Mouse. Demonstrated to react with Human.
Evaluated by Western Blot in mouse brain tissue lysate.
Western Blot Analysis: 1 µg/mL of this antibody detected p53 in 10 µg of mouse brain tissue lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at 2-8°C from date of receipt. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
Immune response to p53 is dependent upon p53/HSP70 complexes in breast cancers. Davidoff, A M, et al. Proc. Natl. Acad. Sci. U.S.A., 89: 3439-42 (1992)
1992
Overexpression of the p53 protein, resulting from gene mutations that increase protein stability, has been detected in greater than 25% of primary human breast cancers. In addition, approximately 10% of breast cancer patients have circulating antibodies to the p53 protein. In this study, the anti-p53 humoral response is correlated with the presence and type of mutant p53 protein expressed in the tumor. In a series of 60 breast cancer patients, 0 of 30 tumors with normal, low-level p53 expression induced anti-p53 antibodies, whereas 7 (23%) of 30 tumors with p53 overexpression elicited a specific anti-p53 antibody response. These 7 patients had anti-p53 antibodies that recognized wild-type p53 and a variety of mutant p53 proteins. A comparison of p53 mutations revealed that antibody-negative tumors had mutations exclusively in exons 7 and 8, whereas antibody-positive tumors had mutations primarily in exons 5 and 6. Moreover, all antibody-eliciting tumors contained complexes between p53 and a 70-kDa heat shock protein, whereas none of the antibody-negative tumors contained this complex. This study implicates a 70-kDa heat shock protein in the antigenic presentation of p53.
p53 mutations, ras mutations, and p53-heat shock 70 protein complexes in human lung carcinoma cell lines. Lehman, T A, et al. Cancer Res., 51: 4090-6 (1991)
1991
The p53 tumor suppressor gene is frequently mutated and the K-ras oncogene is occasionally mutated in primary specimens of human lung carcinomas. These mutated genes also cooperate in the immortalization and neoplastic transformation of rodent cells. To determine whether these mutations are necessary for maintenance of the immortalized and/or neoplastically transformed states of human bronchial epithelial cells, the p53 gene and regions of the ras (K-, H-, and N-) genes were sequenced in nine human lung carcinoma cell lines. Detection of p53 mutations by polymerase chain amplification and direct DNA sequencing was corroborated by p53 immunocytochemistry and coimmunoprecipitation of p53 with heat shock protein 70. p53 and ras genes were frequently, but not always, mutated in the carcinoma cell lines. These data are consistent with the hypothesis that multiple genetic changes involving both protooncogenes and tumor suppressor genes occur during lung carcinogenesis.
Thirty hybridomas that secrete immunoglobulins against the simian virus 40 tumor antigens were isolated and cloned. Of these, 28 produced antibodies which bound to simian virus 40 large-T, and 2 produced antibodies which bound to the host 53,000-dalton protein. As in previous work, large-T antigen was found to have at least one determinant that it shared with small-t antigen and to have a minimum of six unique determinants. Several of the monoclonal antibodies from the L series hybridomas recognized determinants that were present on a subset of the large-T antigen from simian virus 40-transformed mouse cells. These monoclonal antibodies should be useful in studies of the structure and function of the simian virus 40 tumor antigens.
