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Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. Additionally we are shipping Ubiquitin-Like 4A Antibodies (35) and many more products for this protein.
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Human UBL4A Protein expressed in Escherichia coli (E. coli) - ABIN667680
Mariappan, Li, Stefanovic, Sharma, Mateja, Keenan, Hegde: A ribosome-associating factor chaperones tail-anchored membrane proteins. in Nature 2010
Show all 2 references for ABIN667680
ubiquitin-like protein 4A (Ubl4A) plays a crucial role in insulin (show INS Proteins)-induced Akt (show AKT1 Proteins) plasma membrane translocation.
Data indicate that the BAGS domain of BAG6 (Bcl-2-associated athanogene 6 (show BAT3 Proteins)) interacts with the C-terminal domain of Ubl4a (ubiquitin-like protein 4a).
GdX converts TC45, a nonspecific phosphatase, into a STAT3 (show STAT3 Proteins)-specific phosphatase by bridging an association between TC45 and STAT3 (show STAT3 Proteins)
GdX knockout male mice are functionally normal in the reproductive system where Ubl4B was specifically expressed.
Ubl4 gave rise to an autosomal germ cell-specific intronless gene Ubl4b.
The authors identify USP13 (show USP13 Proteins) as a gp78 (show AMFR Proteins)-associated deubiquitinase that eliminates ubiquitin conjugates from Ubl4A to maintain the functionality of Bag6 (show BAT3 Proteins).
Data show that molecular chaperone (show HSP90AA1 Proteins) BAG6_ubiquitin-like domain (UBL) and ubiquitin-like 4A UBL4A_UBL compete for the same binding site on N-terminal dimerisation domain of SGTA (show SGTA Proteins) protein (SGTA_NT).
Both TRC35 (show C7orf20 Proteins) and Ubl4A have distinct C-terminal binding sites on Bag6 (show BAT3 Proteins) defining a minimal Bag6 (show BAT3 Proteins) complex.
Data indicate that BCL2-associated athanogene 6 (BAG6 (show BAT3 Proteins)) appears to be the central component for the process, as depletion of BAG6 (show BAT3 Proteins) leads to the loss of both UBL4A and GET4 (show C7orf20 Proteins) proteins and resistance to cell killing by DNA-damaging agents.
Data indicate that the Bag6 (show BAT3 Proteins)-Ubl4A-Trc35 (show C7orf20 Proteins) complex is localized to the endoplasmic reticulum (ER) membrane to regulate ER-associated degradation (ERAD).
SGTA (show SGTA Proteins) recognizes a noncanonical ubiquitin-like domain in the Bag6 (show BAT3 Proteins)-Ubl4A-Trc35 (show C7orf20 Proteins) complex to promote endoplasmic reticulum-associated degradation.
Structures of the Sgt2 (show PPFIBP1 Proteins)/SGTA (show SGTA Proteins) dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface.
Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region (By similarity).
, ubiquitin-like 4
, ubiquitin-like 4A-like
, ubiquitin-like protein 4A
, housekeeping protein DXS254E
, ubiquitin-like protein GDX
, Ubiquitin-like protein 4A