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M4692-90P MTBP, Human, aa122-139, IN2, Blocking Peptide CAS:

Specifications
References
Grade
Purified
Applications
E WB
EU Commodity Code
38220090
Shipping Temp
Blue Ice
Storage Temp
-20°C

Synthetic peptide (GAVECFEEEDSNSRESLS) corresponding to amino acids 122 to 139 of human MTBP, which differ from the mouse sequence by three amino acids (7).

The p53 tumor-suppressor gene integrates numerous signals that control cell life and death. Several novel molecules involved in p53 network, including Chk2 (1), p53R2 (2), p53AIP1 (3), Noxa (4), PIDD (5), PID/MTA2 (6) and MTBP (7), were recently discovered. The transcriptional activity of p53 is modulated by posttranslational regulations of the p53 protein including stabilization and acetylation. P53 transcriptionally activates MDM2 gene then the translated MDM2 protein binds to p53 and promotes the degradation of p53 leading to lowering the concentration of p53 protein. MDM2 inhibits both p53 mediated G1 arrest and apoptosis. A recently discovered protein termed MTBP was found to bind to MDM2 and to inhibit the modulation effect of MDM2 on p53 (7). MTBP is expressed in a variety of normal tissues (7).
Applications: Suitable for use in ELISA and Western Blot. Other applications not tested.
Storage and Stability: Lyophilized powder may be stored at -20°C. Reconstitute to nominal volume by adding sterile 25% glycerol and store at -20°C. May be stored at 4°C for short-term only. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Source
Synthetic peptide
Purity
Purified
Concentration
~0.2mg/ml
Form
Supplied as a liquid in PBS, pH 7.2, 0.1% BSA, 0.02% sodium azide.
Important Note
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
References
1. Matsuoka S, Huang M, Elledge SJ. Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science. 1998;282:1893–7. 2. Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y. A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature. 2000;404:42–9. 3. Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. Science. 2000;288(5468):1053–8. 4. Oda K, Arakawa H, Tanaka T, Matsuda K, Tanikawa C, Mori T, Nishimori H, Tamai K, Tokino T, Nakamura Y, Taya Y. p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53. Cell. 2000 Sep 15;102(6):849–62. 5. Lin Y, Ma W, Benchimol S. Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis. Nat Genet. 2000;26:122–7. 6. Luo J, Su F, Chen D, Shiloh A, Gu W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature. 2000;408:377–81. 7 Boyd MT, Vlatkovic N, Haines DS. A novel cellular protein (MTBP) binds to MDM2 and induces a G1 arrest that is suppressed by MDM2. J Biol Chem. 2000;275(41):31883–90
USBio References
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