14-3-3 (N19) Antibody-Delta Biolabs

Product Info
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).
Origin	14-3-3 (N19) is provided as an affinity purified rabbit polyclonal antibody, raised against a peptide mapping to the amino terminal domain of human 14-3-3.
Product Details	Each vial contains 200 �g/ml of affinity purified rabbit IgG, 14-3-3 (N19) DB082, in 1 ml PBS containing 0.1 % sodium azide and 0.2% gelatin.
Competition Studies	A blocking peptide is also available, DB082P, for use in competition studies. Each vial contains 0.100 mg of peptide in 0.5 ml PBS with 0.1% sodium azide and 100 mg BSA.
Form	200 �g/ml of rabbit polyclonal IgG in 1 ml PBS containing 0.1 % sodium azide and 0.2% gelatin.
Immunogen	Synthetic peptide mapping to the amino terminal domain of human 14-3-3.
Specificity	14-3-3 (N19) is recommended to detect mouse, rat and human 14-3-3.
Use	Western blotting, immunoprecipitation, and immunohistochemistry (included paraffin embedded tissues). Recommended western blotting starting dilution 1:400. Broadly reactive among the 14-3-3 family, will recognize alpha, beta, zeta (delta) and theta 14-3-3.
Storage	Store this product at 4� C, do not freeze. The product is stable for one year from the date of shipment.
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.