Spheroplast protein Y (spy) Recombinant Protein | spy recombinant protein

Recombinant Escherichia coli Spheroplast protein Y (spy)

Cat. Num. AAA1127774

• Gene Names: spy; ECK1741; JW1732
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Spheroplast protein Y (spy); Recombinant Escherichia coli Spheroplast protein Y (spy); spy 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 Positions: 24-161, full length protein
• Sequence: ADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE
• Sequence Length: 138

• Species: Escherichia coli (strain K12)
• 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 #: 16129697
• NCBI GeneID: 946253
• NCBI Accession #: NP_416257.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P77754
• Molecular Weight: 18,199 Da
• NCBI Official Full Name: periplasmic ATP-independent protein refolding chaperone, stress-induced
• NCBI Official Symbol: spy
• NCBI Official Synonym Symbols: ECK1741; JW1732
• NCBI Protein Information: periplasmic ATP-independent protein refolding chaperone, stress-induced
• UniProt Protein Name: Periplasmic chaperone Spy
• Protein Family: Periplasmic chaperone
• UniProt Gene Name: spy

NCBI Description

Spy is induced by envelope stress, dependent on both CpxR and BaeSR. [More information is available at EcoGene: EG13490]. Expression of spy is regulated by the Cpx envelope stress response as well as by the BaeSR two-component response regulator . [More information is available at EcoCyc: G6939].

Uniprot Description

An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).