重组人DENND1A蛋白
Recombinant Human DENND1A protein
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Recombinant Human DENND1A protein is a Human Full Length protein, in the 1 to 559 aa range, expressed in Wheat germ, suitable for ELISA, WB.
查看别名
FAM31A, KIAA1608, DENND1A, DENN domain-containing protein 1A, Connecdenn 1, Protein FAM31A, Connecdenn
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human DENND1A protein (AB153463)
ab153463 on a 12.5% SDS-PAGE stained with Coomassie Blue.
反应性数据
序列信息
性能和储存信息
运输条件
推荐的短期储存条件
推荐的长期储存条件
分装信息
储存信息
补充信息
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
DENND1A plays an important part in regulating endocytic membrane traffic. It forms part of the multi-protein complex that is responsible for vesicle budding delivery and membrane fusion. This protein aids in mediating the interactions between vesicles and their target membranes ensuring precise and timely transport of cellular materials. Its role in cellular transport highlights the importance of maintaining cellular homeostasis and function.
Pathways
DENND1A participates significantly in the endocytic and exocytic pathways. These pathways control the internalization and secretion of cellular substances important for cellular communication and nutrient uptake. DENND1A influences the function of the Rab GTPases which play a central role in these pathways. Through this interaction DENND1A helps in maintaining the balance between vesicle trafficking and signaling pathways.
特殊说明
形式
Liquid
常规信息
功能
Guanine nucleotide exchange factor (GEF) regulating clathrin-mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles and mediates exit from early endosomes (PubMed : 20154091, PubMed : 20937701). Binds phosphatidylinositol-phosphates (PtdInsPs), with some preference for PtdIns(3)P (By similarity).
翻译后修饰
Phosphorylated on serine and/or threonine in an Akt-dependent manner. Phosphorylation probably regulates the guanine nucleotide exchange factor (GEF) activity, possibly by disrupting an intramolecular interaction between the DENN domain and the C-terminus of the protein, thereby relieving the autoinhibition.
靶点信息
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