KIAA0226
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Official Full Name
KIAA0226 -
Overview
Autophagy is a process of intracellular bulk degradation in which cytoplasmic components including organelles are sequestered within double-membrane vesicles that deliver the contents to the lysosome /vacuole for degradation. Rubicon was identified as Bec -
Synonyms
KIAA0226;run domain Beclin-1 interacting and cystein-rich containing protein;rubicon;RUN domain and cysteine rich domain containing;Beclin 1 interacting protein;rundataxin;baron;beclin-1 associated RUN domain containing protein;RUN domain protein
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| KIAA0226-2428H | Recombinant Human KIAA0226 protein, His-tagged | E.coli | Human | His | 61-290 aa | |
| KIAA0226-406H | Recombinant Human KIAA0226 Protein, MYC/DDK-tagged | HEK293 | Human | DDK&Myc |
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Involved Pathway
KIAA0226 involved in several pathways and played different roles in them. We selected most pathways KIAA0226 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with KIAA0226 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
KIAA0226 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by KIAA0226 itself. We selected most functions KIAA0226 had, and list some proteins which have the same functions with KIAA0226. You can find most of the proteins on our site.
| Function | Related Protein |
|---|
Interacting Protein
KIAA0226 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 KIAA0226 here. Most of them are supplied by our site. Hope this information will be useful for your research of KIAA0226.
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