WDR70
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Official Full Name
WD repeat domain 70 -
Synonyms
WDR70;WD repeat domain 70;WD repeat-containing protein 70;FLJ10233;WD repeat containing protein 70;RGD1309487;4833422F06Rik;MGC109151
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| WDR70-3098C | Recombinant Chicken WDR70 | Mammalian Cell | Chicken | His |
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| WDR70-4128C | Recombinant Chicken WDR70 | Mammalian Cell | Chicken | His |
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| WDR70-6575R | Recombinant Rat WDR70 Protein | Mammalian Cell | Rat | His |
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| WDR70-6231R | Recombinant Rat WDR70 Protein, His (Fc)-Avi-tagged | HEK293 | Rat | His&Fc&Avi |
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| WDR70-6231R-B | Recombinant Rat WDR70 Protein Pre-coupled Magnetic Beads | HEK293 | Rat |
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Involved Pathway
WDR70 involved in several pathways and played different roles in them. We selected most pathways WDR70 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with WDR70 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
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Protein Function
WDR70 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by WDR70 itself. We selected most functions WDR70 had, and list some proteins which have the same functions with WDR70. You can find most of the proteins on our site.
| Function | Related Protein |
|---|
Interacting Protein
WDR70 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with WDR70 here. Most of them are supplied by our site. Hope this information will be useful for your research of WDR70.
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References
- Lehoux, M; Gagnon, D; et al. E1-Mediated Recruitment of a UAF1-USP Deubiquitinase Complex Facilitates Human Papillomavirus DNA Replication. JOURNAL OF VIROLOGY 88:8545-8555(2014).
- Richards, MW; Law, EWP; et al. Crystal structure of EML1 reveals the basis for Hsp90 dependence of oncogenic EML4-ALK by disruption of an atypical beta-propeller domain. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 111:5195-5200(2014).
