

| Numéro de catalogue | 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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| Reactivité des espèces | Saccharomyces cerevisiae (Baker's yeast) | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Espèce hôte | Rabbit | ||||||||
| Clonalité | Polyclonal | ||||||||
| Isotype | IgG | ||||||||
| Immunogène | E. coli - derived recombinant Baker's yeast SSB1 (Met1-Arg613). | ||||||||
| Cible | 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. | ||||||||
| Numéro d'accès | P11484 | ||||||||
| Forme | Liquid | ||||||||
| Tampon de stockage | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
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| Informations d'utilisation du produit |
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| Stabilité et stockage | 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. | ||||||||
| Contexte | 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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