Recombinant Human GDX protein
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Recombinant Human GDX protein is a Human Full Length protein, in the 1 to 157 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
DXS254E, GDX, UBL4, UBL4A, Ubiquitin-like protein 4A, Ubiquitin-like protein GDX
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human GDX protein (AB123144)
12% SDS PAGE, 3 µg of ab123144 loaded.
Reactivity data
Product details
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
Specifications
Form
Liquid
Additional notes
ab123144 was purified using conventional 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). 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).
Post-translational modifications
Polyubiquitinated. Ubiquitination by AMFR and deubiquitination by USP13 may regulate the interaction between the BAG6/BAT3 complex and SGTA and therefore may regulate client proteins fate.
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
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