Product Details

Purity

>85% (SDS-PAGE)

Target Names

SSB1

Uniprot No.

P11484

Alternative Names

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

Species

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

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

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.

Gene References into Functions

A positively charged region in the alpha-helical lid domain of SSB is identified. It is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. PMID: 27882919
Data show that the absence of either Ssb1/2 or Sch9 causes enhanced ribosome aggregation. PMID: 29038496
Study reveals molecular features of chaperone action during translation in eukaryotes by providing proteome-wide Ssb (two isoforms Ssb1 and Ssb2) interaction profiles with nascent chains at near-codon resolution. The Ssb interactome is broader than previously thought and includes nascent mitochondrial and endoplasmic reticulum- (ER) translocated proteins. PMID: 28708998
the ribosome-associated Hsp70 Ssb is redistributed away from Sup35 prion aggregates to the nascent chains, leading to an array of aggregation phenotypes that can mimic both overexpression and deletion of Ssb. PMID: 27828954
Study finds that SSB (i.e. closely related isoforms Ssb1 and Ssb2) binds to a subset of nascent polypeptides whose intrinsic properties and slow translation rates hinder efficient cotranslational folding. PMID: 23332755
The ribosome-bound chaperone system consisting of the ribosome-associated complex (RAC) and the Hsp70 homologs SSB1 and SSB2 are required to stabilize translationally repressed ribosome-polylysine protein complexes. PMID: 23007158
Results suggest that RAC and Ssb1/2p are crucial in maintaining translational fidelity beyond their postulated role as chaperones for nascent polypeptides. PMID: 15456889
ssb and zuo1 have a role in cation influx in Saccharomyces cerevisiae membranes PMID: 15643063
A plausible role of the Ssb1 chaperone is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents. PMID: 16849597
Zuo1 and Ssz1 together with the Hsp70 homolog Ssb1/2 form a functional triad involved in translation and early polypeptide folding processes. PMID: 17901048

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Subcellular Location

Cytoplasm.

Protein Families

Heat shock protein 70 family, Ssb-type Hsp70 subfamily

Database Links

KEGG: sce:YDL229W

STRING: 4932.YDL229W

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Recombinant Saccharomyces cerevisiae Heat shock protein SSB1 (SSB1), partial

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