25 products were found matching "GeneID 22948"!

Protein function: Molecular chaperone, assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin....

Protein function: Molecular chaperone, assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin....

Protein function: Molecular chaperone, assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin....

0.5mg/ml if reconstituted with 0.2ml sterile DI water. CCT5 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides...

TCP1 epsilon is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP dependent...

TCP1 epsilon is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP dependent...

Protein function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC...

Protein function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC...

Host Species: Rabbit. Isotype: IgG. Buffer: Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. Storage: Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Purification Method: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific...

Host Species: Rabbit. Isotype: IgG. Buffer: Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Storage: Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Purification Method: The antibody was affinity-purified from rabbit antiserum by...

Sample Types: serum, plasma, tissue homogenates, cell lysates Detection Range: 15.6 pg/mL-1000 pg/mL Sensitivity: 3.9 pg/mL Assay Principle: quantitative Measurement: SandwichAssay Time: 1-5h Sample Volume: 50-100ulDetection Wavelength: 450 nmProtein function: Component of the chaperonin-containing T-complex (TRiC),...

Protein function: Molecular chaperone, assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin....