SBIR TOPIC 294 PHASE 1 - DEVELOPMENT OF GLYCOSYLATION - SPECIFIC RESEARCH
SBIR TOPIC 294 PHASE 1 - DEVELOPMENT OF GLYCOSYLATION - SPECIFIC RESEARCH
批准号:
8353245
负责人:
YIE-HWA CHANG
金额:
$14.86万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2011
资助国家:
美国
项目状态:
已结题
起止时间:
2011-09-15 至 2012-06-14
关键词:
AntibodiesAntigensBiological AssayCancer BiologyCarbohydratesChickensDevelopmentEarly DiagnosisGlycoproteinsGoalsHumanIgYImageLinkMalignant - descriptorMalignant NeoplasmsMethodsModificationPatternPeptidesPhasePost-Translational Protein ProcessingProtein GlycosylationProteinsReagentResearchResearch PersonnelSiteSmall Business Innovation Research GrantSpecificityStagingTechnologyTestingTimecancer diagnosiscancer therapycancer typeglycosylationinstrumentpolyclonal antibodytumor progression
中文摘要
糖基化改变是恶性转化和肿瘤进展的普遍特征。变化
在大多数人中检测到某些糖蛋白的表达水平和糖基化模式的改变
人类癌症的主要类型和肿瘤进展的不同阶段。早期发现
因此,糖基化变化对癌症的诊断和治疗至关重要。目前,用于
糖基化分析需要昂贵的仪器,而且很耗时。因此,有必要
开发新试剂和更简单的方法来研究癌症中蛋白质的碳水化合物修饰
生物学。我们的长期目标是为基础癌症研究人员开发新的研究试剂,形式为
针对蛋白质中N或O连接的碳水化合物抗原的抗体。在第一阶段的建议中,我们建议
产生32多个鸡多克隆(任务1)和2-3个抗特定糖基化的单抗IgY(任务2)?
网站。此外,我们将使用我们专有的Pincer?平台技术开发5个性价比高的、
利用现有商业产品检测蛋白质糖基化的简单快速方法(任务3)
可用的抗体。我们期望这些钳形试剂不仅可以用来开发
均相分析用于检测蛋白质的糖基化,但也可作为独特的显像剂。
英文摘要
Glycosylation changes are a universal feature of malignant transformation and tumor progression. Changes
in expression levels of certain glycoproteins and altered glycosylation patterns have been detected in most of
the major human cancer types and at different stages of tumor progression. The early detection of
glycosylation changes is therefore crucial for cancer diagnosis and treatment. Currently, the methods for
glycosylation analysis require expensive instruments and are time consuming. Thus, there is a need to
develop new reagents and simpler methods to study carbohydrate modifications of proteins in cancer
biology. Our long term goal is to develop new research reagents for basic cancer researchers in the form of
antibodies against N- or O-linked carbohydrate antigens in proteins. In the Phase I proposal, we propose to
generate over 32 chicken polyclonal (Task 1) and 2-3 monoclonal IgY (Task 2) ¿ against specific Oglycosylation
sites. In addition, we will use our proprietary PINCER¿ platform technology to develop 5 costeffective,
simple and fast assays (Task 3) to detect protein glycosylation using existing commercially
available antibodies. We expect that these PINCER¿ reagents can be used to not only develop
homogeneous assays for detecting protein glycosylation, but can also be used as unique imaging reagents.
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