Human FAS blocking peptide

Name: Human FAS blocking peptide
SKU: CDBP1197
Rating: 5 (1 reviews)

Synthetic Human FAS blocking peptide for Apuri, BL, ELISA

COA

SDS

Datasheet

Summary

Product Overview

Blocking/Immunizing peptide for anti-FAS/CD95 antibody

Target

FAS / CD95

Nature

Synthetic

Tag/Conjugate

Unconjugated

Application Notes

For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not for human or animal consumption.

Format

Lyophilized powder

Preservative

None

Storage

Shipped at ambient temperature, store at -20°C.

Entrez Gene ID

355

Antigen Description

The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. This receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. Several alternatively spliced transcript variants have been described, some of which are candidates for nonsense-mediated mRNA decay (NMD). The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform. [provided by RefSeq, Mar 2011]

Function

identical protein binding; kinase binding; protein binding; receptor activity; signal transducer activity; transmembrane signaling receptor activity;

Synonyms

FAS; Fas cell surface death receptor; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A; TNFRSF6; tumor necrosis factor receptor superfamily member 6; Fas AMA; FAS 827dupA; CD95 antigen; FASLG receptor; apoptosis antigen 1; Delta Fas/APO-1/CD95; FAS receptor variant 9; APO-1 cell surface antigen; TNF receptor superfamily member 6; apoptosis-mediating surface antigen FAS; Fas (TNF receptor superfamily, member 6); tumor necrosis factor receptor superfamily, member 6;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Angiogenic effects of low molecular weight organic acids present in fulvic acids of different sources

NATURAL PRODUCT RESEARCH

Authors: Wang, Zhi; Zhang, Huifen; Qin, Yi; Dai, Weifeng; Li, Baocai; Zhang, Mi

Abstract

Fulvic acid (FA) is a natural mineral medicine with a long medical history in folk. However, the active chemicals of FA remain unknown due to its diversity of sources and the complexity of compositions, which have become a bottleneck in quality control and medicinal development. Based on the traditional effect on angiogenesis, FAs from eight different coal sources were prepared and their active fractions were investigated by the CAM model, resulting that most of acetonitrile dissolved parts of these FAs (DFAs) produced angiogenesis effects. Through chemical analysis on DFAs by GC-FID/MS, six shared organic acids with low molecular weights were identified and quantified, which showed the promoting effects on capillary areas, VEGF, beta-FGF, and Ang-1 at different degrees. The PCA analysis showed that the five shared organic acids with high recognition are the active chemicals in different sources of FAs which may be responsible for the angiogenesis effects.

The AAA plus ATPase valosin-containing protein (VCP)/p97/Cdc48 interaction network in Leishmania

SCIENTIFIC REPORTS

Authors: Aguiar, Bruno Guedes; Dumas, Carole; Maaroufi, Halim; Padmanabhan, Prasad K.; Papadopoulou, Barbara

Abstract

Valosin-containing protein (VCP)/p97/Cdc48 is an AAA+ATPase associated with many ubiquitin-dependent cellular pathways that are central to protein quality control. VCP binds various cofactors, which determine pathway selectivity and substrate processing. Here, we used co-immunoprecipitation and mass spectrometry studies coupled to in silico analyses to identify the Leishmania infantum VCP (LiVCP) interactome and to predict molecular interactions between LiVCP and its major cofactors. Our data support a largely conserved VCP protein network in Leishmania including known but also novel interaction partners. Network proteomics analysis confirmed LiVCP-cofactor interactions and provided novel insights into cofactor-specific partners and the diversity of LiVCP complexes, including the well-characterized VCP-UFD1-NPL4 complex. Gene Ontology analysis coupled with digitonin fractionation and immunofluorescence studies support cofactor subcellular compartmentalization with either cytoplasmic or organellar or vacuolar localization. Furthermore, in silico models based on 3D homology modeling and protein-protein docking indicated that the conserved binding modules of LiVCP cofactors, except for NPL4, interact with specific binding sites in the hexameric LiVCP protein, similarly to their eukaryotic orthologs. Altogether, these results allowed us to build the first VCP protein interaction network in parasitic protozoa through the identification of known and novel interacting partners potentially associated with distinct VCP complexes.