ubl4a Antibody
Description
Role in Actin Branching and Akt Translocation
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Mechanism: UBL4A directly interacts with the Arp2/3 complex to accelerate actin filament branching, forming a network that facilitates protein translocation. For example, insulin stimulation enhances UBL4A-Arp2/3 binding, promoting Akt movement to the plasma membrane for activation .
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Evidence:
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Super-resolution microscopy confirmed colocalization of UBL4A and Arp2/3 in membrane ruffles .
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In vitro actin polymerization assays showed UBL4A enhances Arp2/3-VCA-mediated branching by 30–50% .
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UBL4A knockout (KO) mice exhibited defective glycogen synthesis in neonatal livers due to impaired Akt activation, leading to 60% mortality within 24 hours post-birth .
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Mitochondrial Fusion Under Nutrient Stress
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UBL4A promotes mitochondrial fusion during nutrient deprivation by stabilizing actin branches that support organelle dynamics. KO cells showed fragmented mitochondria and reduced ATP production under starvation .
Comparative Analysis of UBL4A Studies
Applications of UBL4A Antibody in Research
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Western Blot: Detects UBL4A at 17 kDa in mouse, rat, and human tissues .
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Immunofluorescence: Localizes UBL4A to membrane ruffles and lamellipodia, aiding studies on cytoskeletal dynamics .
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Functional Studies: Used to validate UBL4A’s role in glycogen synthesis (via Akt-GSK3β pathway) and mitochondrial health .
Implications and Future Directions
UBL4A antibodies enable critical insights into metabolic regulation and cellular architecture. Future research could explore:
Product Specs
Components: 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
The BAG6/BAT3 complex, of which the target protein is a component, functions as a cytosolic protein quality control complex. It maintains misfolded and hydrophobic proteins in a soluble state, facilitating their delivery to the endoplasmic reticulum (ER) or targeting them for proteasomal degradation. This complex is crucial for the post-translational delivery of tail-anchored and type II transmembrane proteins to the ER membrane. Furthermore, it acts as a sorting platform for mislocalized secretory pathway proteins, directing them either to the proteasome for degradation or to the ER for proper localization. The BAG6/BAT3 complex also participates in ER-associated degradation (ERAD), a quality control mechanism removing unwanted ER proteins. This involves retrotranslocation to the cytosol and subsequent proteasomal targeting. The complex keeps these retrotranslocated proteins in a soluble, unfolded state, ensuring efficient proteasomal delivery.
