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Antennapedia Peptide Sale

(Synonyms: 黑腹果蝇触足肽) 目录号 : GC33336

AntennapediaPeptide是由16个氨基酸残基组成的多肽,来源于果蝇转录因子Antennapedia的60个氨基酸序列的同源域,它同时是一种穿膜肽。

Antennapedia Peptide Chemical Structure

Cas No.:188842-14-0

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1mg
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5mg
¥3,213.00
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产品描述

Antennapedia Peptide is a 16 amino acid peptide, originally derived from the 60 amino acid long homeodomain of the Drosophila transcription factor Antennapedia and is a member of the family of Cell-penetrating peptides.

Antennapedia (Antp)-SMCC-cytochrome c conjugate (5 μg/mL) activates caspase-dependent apoptosis of HeLa cells. The Antp-SMCC-cytochrome c conjugate reduces the clonogenic survival of Hela cells, and inhibits clonogenic survival[1]. ANTP-SmacN7 fusion protein can transduce and accumulate in cells, while SmacN7 alone cannot. ANTP-SmacN7 fusion proteins have a radiation-sensitising effect on EC109 cells. ANTP-SmacN7 combined with radiation does not promote further increases in caspase-3 protein expression, it increases the levels of cleaved caspase-3[2].

[1]. Imesch P, et al. Conjugates of cytochrome c and antennapedia peptide activate apoptosis and inhibit proliferation of HeLa cancer cells. Exp Ther Med. 2013 Sep;6(3):786-790. Epub 2013 Jul 4. [2]. Du LQ, et al. Radiation-sensitising effects of antennapedia proteins (ANTP)-SmacN7 on tumour cells. Int J Mol Sci. 2013 Dec 11;14(12):24087-96.

Chemical Properties

Cas No. 188842-14-0 SDF
别名 黑腹果蝇触足肽
Canonical SMILES Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys
分子式 C104H168N34O20S 分子量 2246.8
溶解度 Soluble in Water 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 0.4451 mL 2.2254 mL 4.4508 mL
5 mM 0.089 mL 0.4451 mL 0.8902 mL
10 mM 0.0445 mL 0.2225 mL 0.4451 mL
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Research Update

A 16-mer peptide (RQIKIWFQNRRMKWKK) from antennapedia preferentially targets the Class I pathway

Vaccine 2001 Jan 8;19(11-12):1397-405.PMID:11163662DOI:10.1016/s0264-410x(00)00373-x.

Translocation of antigenic peptides into the cytosol of antigen presenting cells facilitates proteosomal processing and loading into Class I molecules for MHC presentation on the cell surface. The DNA binding domain of the Drosophila transcription factor (Antennapedia), a 60 amino acid protein, is rapidly taken up by cells and has been fused to selected antigens to enhance their immunogenicity. We now demonstrate that a 16 amino acid peptide from antennapedia can facilitate the cytoplasmic uptake of CTL epitope 9-mer peptides. Synthetic peptides were made containing the 16-mer Antennapedia Peptide linked in tandem to the ovalbumin SIINFEKL CTL peptide. The peptide complex was shown to rapidly internalise into APCs by confocal microscopy. This peptide induced CTL in C57BL/6 mice and protected them against growth of an ovalbumin expressing tumour cell line (E.G7-OVA). The ability of the hybrid peptide to be processed and presented by APCs was similar, whether the SIINFEKL sequence was appended at the C-terminus or N-terminus of the Antennapedia Peptide. The production of synthetic peptides containing other CTL peptide epitopes may be useful for priming CTLs in vitro and in vivo

The Antennapedia Peptide penetratin translocates across lipid bilayers - the first direct observation

FEBS Lett 2000 Oct 6;482(3):265-8.PMID:11024473DOI:10.1016/s0014-5793(00)02072-x.

The potential use of polypeptides and oligonucleotides for therapeutical purposes has been questioned because of their inherently poor cellular uptake. However, the 16-mer oligopeptide penetratin, derived from the homeodomain of Antennapedia, has been reported to enter cells readily via a non-endocytotic and receptor- and transporter-independent pathway, even when conjugated to large hydrophilic molecules. We here present the first study where penetratin is shown to traverse a pure lipid bilayer. The results support the idea that the uptake mechanism involves only the interaction of the peptide with the membrane lipids. Furthermore, we conclude that the translocation does not involve pore formation.

AP-4F, Antennapedia Peptide linked to an amphipathic alpha helical peptide, increases the efficiency of Lipofectamine-mediated gene transfection in endothelial cells

Biochem Biophys Res Commun 2003 Jun 6;305(3):605-10.PMID:12763037DOI:10.1016/s0006-291x(03)00803-9.

Typically, endothelial cells are difficult to transfect. In this study, we report that Antennapedia Peptide (AP) linked to L-4F, a water-soluble, amphipathic alpha helical peptide that avidly binds lipids (AP-4F) increases Lipofectamine 2000-mediated transfection of bovine coronary endothelial cell cultures. Transfection efficiency was monitored by flow cytometry and fluorescent microscopy. Lipofectamine 2000 transfection of endothelial cell cultures with green fluorescence protein (GFP)-DNA typically yields transfection efficiencies of 35.4+/-3.3% with low levels of cell death (8.1+/-1.0%). Pre-treatment of the Lipofectamine 2000-GFP-DNA complexes with AP-4F for 5 min increased transfection to 58.2+/-2.8% without increasing cell death. AP-4F increases Lipofectamine 2000-mediated transfection in a time-dependent fashion (within 10-20 min). Systematic studies reveal that the individual components of AP-4F, i.e., AP and L-4F alone, are ineffective in increasing Lipofectamine 2000-mediated transfection and that AP-4F must be directly associated with DNA liposomes prior to transfection for optimal uptake by endothelial cells. These observations demonstrate that AP-4F may be useful for increasing the transfection efficiency of endothelial cell cultures with standard commercially available reagents.

Conjugates of cytochrome c and Antennapedia Peptide activate apoptosis and inhibit proliferation of HeLa cancer cells

Exp Ther Med 2013 Sep;6(3):786-790.PMID:24137266DOI:10.3892/etm.2013.1205.

Polycationic cell-penetrating peptides (CPPs) deliver macromolecules into cells without losing the functional properties of the cargoed macromolecule. The aim of this study was to determine whether exogenous cytochrome c is delivered to HeLa cervical carcinoma cells by the CPP antennapedia (Antp) and activates apoptosis. HeLa cervical carcinoma cells were treated with conjugated Antp-SMCC-cytochrome c (cytochrome c chemically conjugated to Antp) or with non-conjugated Antp and cytochrome c. Sensitivity to the treatments was determined by the clonogenic assay (proliferation) and by immunoblot analysis (apoptosis activation). We report that conjugated Antp-SMCC-cytochrome c activated apoptosis in HeLa cells as demonstrated by poly (ADP-ribose) polymerase 1 (PARP-1) cleavage and inhibited their proliferation. The Antp-SMCC-cytochrome c-induced apoptosis was inhibited by z-VAD-fmk, a pan-caspase inhibitor peptide. Unconjugated Antp or cytochrome c demonstrated no inhibitory effect on survival and proliferation. Our results suggest that chemical coupling of cytochrome c to CPPs may present a possible strategy for delivering cytochrome c into cells and for activating apoptosis.

Genomic DNA recombination with cell-penetrating peptide-tagged cre protein in mouse skeletal and cardiac muscle

Genesis 2014 Jul;52(7):695-701.PMID:24753043DOI:10.1002/dvg.22782.

The Cre-loxP recombination system has been used to promote DNA recombination both in vitro and in vivo. For in vivo delivery, Cre expression is commonly achieved through the use of tissue/cell type-specific promoters, viral infection, or drug inducible transcription and protein translocation to promote targeted DNA excision. The development of cell permeable (or penetrating) peptide tagged proteins has facilitated the delivery of Cre recombinase protein into cells in culture, organotypic slide culture, or in living animals. In this report, we generated bacterially expressed, his-tagged Cre protein with either a cardiac targeting peptide or an Antennapedia Peptide at the C-terminus and demonstrated efficient uptake and recombination in both cell culture and mice. To facilitate delivery to cardiac and skeletal muscle, we mixed proteins with pluronic F-127 hydrogel and delivered Cre protein into reporter Rosa26mTmG mouse skeletal muscle or Rosa26LacZ cardiac muscle via ultrasound guided injection. Activation of reporter gene expression indicated that these Cre proteins were enzymatically active. Recombination events were detected only in the vicinity of injection areas. In conclusion, we have developed a method to deliver enzymatically active Cre protein locally to skeletal muscle and cardiac muscle that may be adapted for use with other proteins.