

| Catalog No. | JN840014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Description |
Anti-Baker's yeast SSB1 Polyclonal Antibody (JN840014) is a rabbit polyclonal antibody detecting SSB1 in ELISA, IHC, WB.
Highlights
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| Species reactivity | Saccharomyces cerevisiae (Baker's yeast) | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Baker's yeast SSB1 (Met1-Arg613). | ||||||||
| Target | Ribosome-associated molecular chaperone SSB1, 3.6.4.10, Cold-inducible protein YG101, Heat shock protein SSB1, Hsp70 chaperone Ssb, SSB1, YG101, YDL229W | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | P11484 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Background | Ribosome-associated molecular chaperone SSB1 is a ~66 kDa protein. 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. | ||||||||
| Note | For research use only. |
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