E. coli Host Cell Protein Standards
- Known as:
- E. coli Host Cell Protein Standards
- Catalog number:
- AB000106
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- Array Bridge
- Gene target:
- . coli Host Cell Protein Standards
Related genes to: E. coli Host Cell Protein Standards
- Gene:
- FCN2 NIH gene
- Name:
- ficolin 2
- Previous symbol:
- -
- Synonyms:
- P35, FCNL, EBP-37, ficolin-2
- Chromosome:
- 9q34.3
- Locus Type:
- gene with protein product
- Date approved:
- 1996-07-11
- Date modifiied:
- 2016-10-05
Related products to: E. coli Host Cell Protein Standards
Related articles to: E. coli Host Cell Protein Standards
- Poly(ethylene glycol) (PEG) is widely used in nanomedicine design, but emerging PEG immunogenicity in the general population is of therapeutic concern. As alternative, polyoxazolines are gaining popularity, since "polyoxazolinated" nanoparticles show long-circulating properties comparable to PEGylated nanoparticles in mice. Here, we show species differences in opsonization and differential uptake by monocytes and macrophages of nanoparticles coated with either poly-2-methyl-2-oxazoline or poly-2-ethyl-2-oxazoline. These nanoparticles evade murine opsonization process and phagocytic uptake but porcine ficolin 2 (FCN2), through its S2 binding site, recognizes polyoxazolines, and mediates nanoparticle uptake exclusively by porcine monocytes. In human sera, FCN opsonization is isoform-dependent showing inter-individual variability but both FCN2 and complement opsonization promote nanoparticle uptake by human monocytes. However, nanoparticle uptake by human and porcine macrophages is complement-dependent. These findings advance mechanistic understanding of species differences in innate immune recognition of nanomaterials' molecular patterns, and applicable to the selection and chemical design of polymers for engineering of the next generation of stealth nanoparticles. - Source: PubMed
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Tavano RMorillas-Becerril LGeffner-Smith ARonzani GGervasutti RArrigoni GBattisti IMorbidelli MPolverino de Laureto PPalazzi LNatale ASchiavon ECoin PBenetti E MRomio MCorzana FJiménez-Moreno ESturlese MBolcato GMoro SMoghimi S MMancin FPapini E - Acute myocardial infarction (AMI) is a critical cardiovascular event characterized by sudden coronary blood flow interruption, leading to myocardial ischemia and necrosis. Despite advances in acute therapeutic measures, understanding the metabolic damage related to AMI, particularly through specific protein expressions, remains limited. This study utilized Olink cardiovascular metabolomics technology to explore cardiovascular metabolism-related protein biomarkers associated with AMI, aiming to address the clinical need for early diagnosis and targeted therapy. - Source: PubMed
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Zeng XuemeiSehrawat AnuradhaLafferty Tara KChen YijunRawat MahikaKamboh M IlyasVillemagne Victor LLopez Oscar LCohen Ann DKarikari Thomas K - This study was to explore the relationship between plasma exosomes and Acute myocardial infarction (AMI). - Source: PubMed
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