Recombinant Human Elongin B/Elongin C/VHL Complex, CF Summary
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins.Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration.The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard.In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
E3-600
| Formulation | X mg/ml (XμM) in 50 mM HEPES pH 7.5, 200 mM NaCl, 10% (v/v) Glycerol, 2 mM DTT |
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| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: ELOB/ELOC/VHL Complex
Together, Elongin B (ELOB) and Elongin C (ELOC) form a heterodimer that serves as the regulatory subunit for the Elongin complex--a general transcription elongation factor that increases RNA Polymerase II transcription through template-encoded arresting sites. The ELOB/ELOC complex also binds to the "BC-box motif" found in many proteins in the VHL-box and SOCS-box protein families. In this function, ELOB/ELOC serves as an adapter between substrate recognition proteins and either Cullin-2/Rbx1 (in VHL-box E3 Ubiquitin ligases) or Cullin-5/Rbx2 (in SOCS-box E3 Ubiquitin ligases). VHL (von Hippel-Lindau disease tumor suppressor) is the substrate recognition subunit for an E3 ligase activity that ubiquitinates proteins containing hydroxyproline residues. Targets of VHL include HIF1alpha, beta 2 adrenergic receptor, ZHX2 and others. This protein complex is untagged.
- Kamura T., et al. (1998) Genes & Dev. doi:10.1101/gad.12.24.3872
- Okumura F., et al. (2012) Front. Oncol. doi:10.3389/fonc.2012.00010
- Xie L., et al. (2009) Sci. Signaling doi:10.1126/scisignal.2000444
- Zhang J. et al. (2018) Science doi:10.1126/science.aap8411
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炎性体（inflammasome）是细胞内的一类多蛋白复合物，在炎性反应中发挥着至关重要的作用。炎性体包括半胱天冬酶-1（caspase1）、PYCARD和NALP，有时也包括半胱天冬酶-5（caspase5，也被称作半胱天冬酶-11或ICH-3）。它是在骨髓细胞（myeloidcell）中产生的，也是先天性免疫系统的一个组分。炎性体的确切组成依赖于启动炎性体组装的激活物，如双链RNA和石棉会引发不同的炎性体组成。炎性体促进炎性细胞因子IL-1β和IL-18成熟。
在一项新的研究中，来自比利时法兰德斯生物技术中心/根特大学（VIB/UGent）的LieselotteVandeWalle博士、DanielJiménezFernández以及教授MoLamkanfi研究团队对半胱天冬酶-12（caspase12）的功能产生新的认识。基于此，他们打破了这个领域对半胱天冬酶-12的固执观念：半胱天冬酶-12是炎性体的负调节物。这些新的认识为研究人员挣脱现有的研究路线和鉴定它的真正生理学功能铺平道路。相关研究结果发表在2016年6月2日那期Nature期刊上，论文标题为“Doescaspase-12suppressinflammasomeactivation?”。
研究人员也指出这将需要进行大量的“重新研究（re-researching）”。之前所谓的半胱天冬酶-12在细胞死亡、应激反应、疟疾和败血症等中的作用---引用了9000多次---必需复核，这是因为这些作用经常是基于不正确的小鼠模型得出的。
VIB/UGent教授MoLamkanfi说，“我们发现在很多情形下，对半胱天冬酶-12的研究是基于对半胱天冬酶-11（caspase11）和半胱天冬酶-12都进行基因敲除的小鼠模型开展的。因此从研究结果中推断半胱天冬酶-12的作用是不可能的。我们如今引入新的选择性半胱天冬酶-12基因敲除小鼠，这应当能够让我们追踪半胱天冬酶-12的确切功能。”
利用这些新的小鼠，Lamkanfi团队证实在体外模拟的BMDM（bonemarrow-derivedmacrophage,骨髓衍生性巨噬细胞）和体内接种的小鼠中，半胱天冬酶-12缺乏都不能增加半胱天冬酶-1激活。剔除半胱天冬酶-12也不会增强炎性体途径释放出成熟的IL-1β和IL-18。他们的发现表明不论半胱天冬酶-11的表达状态如何，半胱天冬酶-12都不会作为半胱天冬酶-1激活的生理学上负显性调节物，因而也不会作为炎性体的生理学上负显性调节物。
明白了么，少年？
