Heat shock protein SSB2 (SSB2) Recombinant Protein | SSB2 recombinant protein

Recombinant Saccharomyces cerevisiae Heat shock protein SSB2 (SSB2) , partial

• Gene Names: SSB2; YG103
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Heat shock protein SSB2 (SSB2); Recombinant Saccharomyces cerevisiae Heat shock protein SSB2 (SSB2); partial; SSB2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Length: 613

• Species: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

NCBI and Uniprot Product Information

• NCBI GI #: 6324120
• NCBI GeneID: 855512
• NCBI Accession #: NP_014190.1
• NCBI GenBank Nucleotide #: NM_001183047.1
• UniProt Accession #: P40150; D6W0Y1
• Molecular Weight: 66,595 Da
• NCBI Official Full Name: Hsp70 family ATPase SSB2
• NCBI Official Symbol: SSB2
• NCBI Official Synonym Symbols: YG103
• NCBI Protein Information: Hsp70 family ATPase SSB2
• UniProt Protein Name: Ribosome-associated molecular chaperone SSB2
• Protein Family: Heat shock protein
• UniProt Gene Name: SSB2

Uniprot Description

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.