Recombinant E. coli slyD protein (Tag Free)
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Recombinant E. coli slyD protein (Tag Free) is a Escherichia coli CFT073 Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
c4123, slyD, FKBP-type peptidyl-prolyl cis-trans isomerase SlyD, PPIase, Metallochaperone SlyD
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant E. coli slyD protein (Tag Free) (AB72847)
SDS-PAGE showing ab72847 (3μg) at approximately 21kDa.
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
The SlyD protein serves important roles in cellular homeostasis by assisting in protein folding and stabilization of cellular stress responses. It acts independently as well as a component of larger protein complexes. Its activity aids in maintaining the functionality of unfolded or misfolded proteins that might otherwise aggregate which is important for preventing cellular stress and potential damage.
Pathways
SlyD plays an important role in the protein homeostasis and stress response pathways. It engages in cellular processes related to the cellular stress response especially as it connects with heat shock proteins like Hsp70. SlyD also associates with proteins part of the folding pathway supporting both protein synthesis under normal conditions and recovery during stress.
Specifications
Form
Liquid
Additional notes
ab72847 is purified by conventional chromatography.
General info
Function
Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in Tat-dependent translocation, by binding to the Tat-type signal of folded proteins (By similarity).. Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity (By similarity).
Sequence similarities
Belongs to the FKBP-type PPIase family.
Target data
Additional targets
Complementary Products
Product promise
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