Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release. .

p11484

Ribosome-associated molecular chaperone SSB1 (EC 3.6.4.10) (Cold-inducible protein YG101) (Heat shock protein SSB1) (Hsp70 chaperone Ssb),SSB1 YG101 YDL229W,Ribosome-associated molecular chaperone SSB1, 3.6.4.10, Cold-inducible protein YG101, Heat shock protein SSB1, Hsp70 chaperone Ssb, SSB1, YG101, YDL229W

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)

WB,IHC,ELISA

WB 1:500-1:2000
IHC 1:50-1:300
ELISA 1:5000-1:20000

67kD

Rabbit

Recombinant Baker's yeast SSB1 (Met1-Arg613).

Polyclonal

IgG

Purified by antigen affinity column.

0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4℃ short term (1-2 weeks). Store at -20℃ 12 months.