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TAT 48-57 Sale

目录号 : GC32320

TAT(48-57)是可渗透细胞膜的一种多肽,来源于HIV-1反式激活因子(Tat)的第48-57位氨基酸残基。

TAT 48-57 Chemical Structure

Cas No.:253141-50-3

规格 价格 库存 购买数量
1mg
¥714.00
现货
5mg
¥1,607.00
现货
10mg
¥2,499.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

TAT (48-57) is a cell-permeable peptide, derived from HIV-1 transactivator of transcription (Tat) protein residue 48-57.

TAT (48-57) is a cell-permeable peptide with short length, good at crossing cell membranes of different cell types, with overall low toxicity, and does not leak out from cells once internalised[1].

[1]. Cardozo AK, et al. Cell-permeable peptides induce dose- and length-dependent cytotoxic effects. Biochim Biophys Acta. 2007 Sep;1768(9):2222-34.

Chemical Properties

Cas No. 253141-50-3 SDF
Canonical SMILES Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg
分子式 C55H109N31O12 分子量 1396.65
溶解度 DMSO : 50 mg/mL (35.80 mM; Need ultrasonic) 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 0.716 mL 3.58 mL 7.16 mL
5 mM 0.1432 mL 0.716 mL 1.432 mL
10 mM 0.0716 mL 0.358 mL 0.716 mL
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Research Update

In Situ Tissue Labeling of Cerebral Amyloid Using HIV-Related Tat Peptide

Mol Neurobiol 2018 Aug;55(8):6834-6840.PMID:29349578DOI:10.1007/s12035-018-0870-x.

Delivering peptide-based drugs to the brain is a major challenge because of the existence of the blood-brain barrier (BBB). To overcome this problem, cell-penetrating peptides derived from proteins that are able to cross biological membranes have been used as cell-permeable and brain-penetrant compounds. An example is the transactivator of transcription protein transduction domain (Tat) of the human immunodeficiency virus. The basic domain of Tat is formed of arginine and lysine amino acid residues. Tat has been used as brain-penetrant carrier also in therapies for Alzheimer disease (AD), the most common form of dementia characterized by extracellular cerebral deposits of amyloid made up of Aβ peptide. The aim of our study was to assess whether Tat bind to amyloid deposits of AD and other amyloidoses. An in situ labeling using biotinylated TAT 48-57 peptide was employed in the brain tissue with amyloid deposits made up of Aβ (patients with AD and transgenic AD mice), of prion protein (patients with Gerstmann-Straussler-Scheinker disease), and other amyloidosis, processed by different fixations and pretreatments of histological sections. Our results showed that Tat peptide binds amyloid deposits made up of Aβ, PrP, and immunoglobulin lambda chains in the brain and other tissues processed by alcoholic fixatives but not in formalin-fixed tissue. The fact that biotinylated Tat peptide stains amyloid of different biochemical composition and the specific charge characteristics of the molecules suggests that Tat may bind to heparan sulfate glicosaminoglicans, that are present in amyloid deposits. Inhibition of the binding by Tat pre-incubation with protamine reinforces this hypothesis. Binding of Tat to amyloid deposits should be kept in mind in interpreting the results of studies employing this molecule as brain-penetrating compound for the treatment of cerebral amyloidoses. Our results also suggest that Tat may be helpful for the analysis of the mechanisms of amyloidogenesis, and in particular, the interactions between specific amyloid peptides and glicosaminoglicans.

Photochemical internalisation of a macromolecular protein toxin using a cell penetrating peptide-photosensitiser conjugate

J Control Release 2012 Jan 30;157(2):305-13.PMID:21889554DOI:10.1016/j.jconrel.2011.08.025.

Photochemical internalisation (PCI) is a site-specific technique for improving cellular delivery of macromolecular drugs. In this study, a cell penetrating peptide, containing the core HIV-1 TAT 48-57 sequence, conjugated with a porphyrin photosensitiser has been shown to be effective for PCI. Herein we report an investigation of the photophysical and photobiological properties of a water soluble bioconjugate of the cationic Tat peptide with a hydrophobic tetraphenylporphyrin derivative. The cellular uptake and localisation of the amphiphilic bioconjugate was examined in the HN5 human head and neck squamous cell carcinoma cell line. Efficient cellular uptake and localisation in endo/lysosomal vesicles was found using fluorescence detection, and light-induced, rupture of the vesicles resulting in a more diffuse intracellular fluorescence distribution was observed. Conjugation of the Tat sequence with a hydrophobic porphyrin thus enables cellular delivery of an amphiphilic photosensitiser which can then localise in endo/lysosomal membranes, as required for effective PCI treatment. PCI efficacy was tested in combination with a protein toxin, saporin, and a significant reduction in cell viability was measured versus saporin or photosensitiser treatment alone. This study demonstrates that the cell penetrating peptide-photosensitiser bioconjugation strategy is a promising and versatile approach for enhancing the therapeutic potential of bioactive agents through photochemical internalisation.