MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

Pureté

Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.(c) Analysis by SDS-PAGE.

Forme du produit

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

Lyophilized from a 0.2Âµm filtered concentrated solution in PBS, pH 7.2.

Stockage

Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Synonymes

APC1, APC1 protein, Cachectin, DIF, Differentiation inducing factor, Macrophage cytotoxic factor, soluble form, Tnf, TNF alpha, TNF macrophage derived, TNF monocyte derived, TNF superfamily member 2 , TNF superfamily, member 2, TNF, macrophage derived, TNF, monocyte derived, TNF-a, TNF-alpha, TNFA, TNFA_HUMAN, TNFSF2, Tumor necrosis factor, Tumor necrosis factor (TNF superfamily member 2) , Tumor necrosis factor alpha, Tumor necrosis factor ligand superfamily member 2, Tumor Necrosis Factor, Membrane Form, Tumor necrosis factor, soluble form

Avertissement

Ce produit est uniquement destiné à la recherche. Il n'est pas destiné à un usage diagnostique ou thérapeutique.

Références (1)

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(7)

PUMA is directly activated by NF-kappaB and contributes to TNF-alpha-induced apoptosis.

Références : TNF a Mouse (A61685)

Résumé :

Tumor necrosis factor-alpha (TNF-alpha) is a cytokine that has an important role in immunity and inflammation by inducing cellular responses such as apoptosis. The transcription factor nuclear factor-kappaB (NF-kappaB) can paradoxically suppress and promote apoptosis in response to TNF-alpha. In this study, we found that p53 upregulated modulator of apoptosis (PUMA), a p53 downstream target and a BH3-only Bcl-2 family member, is directly regulated by NF-kappaB in response to TNF-alpha. TNF-alpha treatment led to increases in PUMA mRNA and protein levels in human colon cancer cells. The induction of PUMA was p53 independent, and mediated by the p65 component of NF-kappaB through a kappaB site in the PUMA promoter. The apoptotic effect of PUMA induction by TNF-alpha was unmasked by depleting the antiapoptotic protein Bcl-X(L). In mice, PUMA was also induced by TNF-alpha in an NF-kappaB-dependent manner. TNF-alpha-induced apoptosis in a variety of tissues and cell types, including small intestinal epithelial cells, hepatocytes, and thymocytes, was markedly reduced in PUMA-deficient mice. Collectively, these results demonstrated that PUMA is a direct target of NF-kappaB and mediates TNF-alpha-induced apoptosis in vitro and in vivo.

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