23-044-M
VHL Protein Complex, Active, 10 µg
Active complex of five (5) recombinant human enzymes: VHL amino acids 54-end, full length Elongin C, full length Elongin B, full length Cul2, & full length Rbx1. For use in Enzyme Assays. Functions as an E3 ligase in ubiquitination assays.
别名:
VCB-Cul2 complex, ECV complex, CBC VHL
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About This Item
生物来源
human
质量水平
重组
expressed in Sf21 cells
形式
liquid
制造商/商品名称
Upstate®
技术
activity assay: suitable
溶解性
water: soluble
基因信息
human ... Cul2(8453) , Rbx1(9978) , VHL(7428)
一般描述
The VHL complex is a multi-subunit ubiquitin ligase composed of VHL, Elongin B, Elongin C, Cul2 and Rbx1. The VHL protein serves as the substrate recognition component and is linked by Elongin C to a heterodimeric Cul2/Rbx1 module that functions as a potent activator of the ubiquitination of target proteins by an E2 conjugating enzyme. Elongin B interacts with the complex through Elongin C and appears to stabilize the binding of Elongin C to VHL. The primary function of the VHL complex is to regulate HIF (hypoxia inducible factor) activity by targeting the hydroxylated HIF-1α subunit for ubiquitination and rapid proteasomal degradation under normoxic conditions. It therefore plays an important role in the regulation of hypoxia-inducible genes such as the vascular endothelial growth factor (VEGF) and glucose transport-1 (Glut-1). Mutations in VHL are associated with the inherited von Hippel-Lindau (VHL) cancer syndrome and numerous forms of renal cell carcinoma.
应用
Ubiquitination Cascade Comoponent: E3
外形
Purified using glutathione sepharose.
其他说明
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
法律信息
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
免责声明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Molecular cell, 79(3), 376-389 (2020-07-09)
Activation of dual-specificity tyrosine-phosphorylation-regulated kinases 1A and 1B (DYRK1A and DYRK1B) requires prolyl hydroxylation by PHD1 prolyl hydroxylase. Prolyl hydroxylation of DYRK1 initiates a cascade of events leading to the release of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase
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