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14-3-3 antibody


Rabbit Polyclonal anti-14-3-3



Catalog Number: NB100-2140
Price: $325.00 Add to cart
 

Background:

14-3-3 family of proteins is composed of seven isotypes, beta, gamma, zeta, epsilon, tau, eta, and sigma, that play critical roles in cell signaling events that control cell cycle progression, transcriptional alterations, and apoptosis (1-4). 14-3-3 proteins were the first signaling molecules to be identified as specific phosphoserine/threonine binding proteins (1). 14-3-3 can serve as a direct regulator of its target by altering the function of the protein (3). 14-3-3 protein targets include the signalling intermediates Raf, MEKK, PI-3 kinase and IRS-1, cell cycle proteins CDK2, Wee1, and Cdc25, and apoptosis proteins BAD and ASK-1 (3,4).



Host:

Rabbit



Research Areas:

Signal Transduction, Growth and Development, Neuronal Markers, IHC Grade



Immunogen:

Synthetic peptide mapping to the amino terminal domain of human 14-3-3.



Isotype:

IgG



Specificity:

Broadly reactive among the 14-3-3 family. This antibody recognizes alpha, beta, zeta (delta) and theta 14-3-3.



Localization:

Cytoplasmic



Species Reactivity:

Cross-reacts with Human, Mouse and Rat. Not yet tested in other species.
Other species have not been tested.



Dilutions:

Suggested working dilutions *
immunohistochemistry ,
immunoprecipitation ,
Western Blot 1/400
* Investigator should determine optimal working dilutions.



Positive Controls:

HeLa and Jurkat whole cell lysates.
* Hela Whole Cell Lysate NB800-PC1
* Jurkat Whole Cell Lysate NB800-PC2



Packaging:

1 ml Immunogen affinity purified Rabbit antisera.



Concentration:

0.2 mg/ml



Buffer:

0.2% Gelatin, PBS



Preservative:

0.1% Sodium Azide



Storage:

Store at 4C. Do not freeze.



Limitations:

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 6 months from date of receipt.



General References:

1. Yaffe MB. 2002. How do 14-3-3 proteins work?- - Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513(1):53-57.
2. Liu MY, Cai S, Espejo A, Bedford MT, Walker CL. 2002. 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation sites. Cancer Res. 62(22): 6475-6480.
3. Tzivion G, Shen YH, Zhu J. 2001. 14-3-3 proteins; bringing new definitions to scaffolding. Oncogene 20(44):6331-6338.
4. Fu H, Subramanian RR, Masters SC. 2000. 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol. 40:617-647.



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