Recombinant Human CEE protein (His tag) (denatured)
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Recombinant Human CEE protein (His tag) (denatured) is a Human Full Length protein, in the 1 to 327 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
C7orf20, CEE, TRC35, CGI-20, GET4, Golgi to ER traffic protein 4 homolog, Conserved edge-expressed protein, Transmembrane domain recognition complex 35 kDa subunit
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human CEE protein (His tag) (denatured) (AB177608)
15% SDS-PAGE analysis of ab177608 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CEE influences cell signaling and metabolic processes. It functions within a larger protein complex regulating transcription factors critical in gene expression. This involvement allows CEE to influence adaptation and response mechanisms within the cell contributing to cellular homeostasis.
Pathways
The protein CEE participates in signal transduction and metabolic pathways. It interacts with kinase proteins like MAPK in the signaling pathway to mediate cell growth and survival. Through the metabolic pathway CEE supports various enzymatic activities linking it to the broader metabolic network within cells.
Specifications
Form
Liquid
Additional notes
ab177608 was purified using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography.
General info
Function
As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed : 20676083, PubMed : 21636303, PubMed : 21743475, PubMed : 28104892, PubMed : 32395830). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed : 20676083, PubMed : 25535373, PubMed : 28104892). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome (PubMed : 28104892). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed : 21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed : 21636303).
Sequence similarities
Belongs to the GET4 family.
Post-translational modifications
Ubiquitinated by RNF12, leading to proteasomal degradation. When unassembled from BAG6; ubiquitinylation is modulated by BAG6 quality control role and effectuated by RNF126.
Target data
Product promise
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