Recombinant 50S ribosomal protein L22 (rplV)

• Purity: >85% (SDS-PAGE)
• Host Species: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Accession: P61182
• Gene: rplV
• CAT.NO: B000135
• Expression Systems: E.coli In Vivo Biotinylation in E.coli Yeast Baculovirus Mammalian cell
• Product Name: Recombinant 50S ribosomal protein L22 (rplV)
• Source: E.coli;In Vivo Biotinylation in E.coli;Yeast;Baculovirus;Mammalian cell
• Protein Expression Range: 1-114
• Tag: Tag type will be determined during the manufacturing process.
• Form: Lyophilized powder
• Buffer: Tris/PBS-based buffer, 6% Trehalose.
• Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
• Alternative Names: rplV; SP_0214; 50S ribosomal protein L22
• Target Protein Sequence: MAEITSAKAM ARTVRVSPRK SRLVLDNIRG KSVADAIAIL TFTPNKAAEI ILKVLNSAVA NAENNFGLDK ANLVVSEAFA NEGPTMKRFR PRAKGSASPI NKRTAHITVA VAEK
• Protein Length: full length protein
• 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.
• 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.
• Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

This protein specifically binds to 23S rRNA, a process facilitated by interactions with other ribosomal proteins such as L4, L17, and L20. It plays a crucial role in the early stages of 50S subunit assembly. Once assembled, it forms multiple contacts with different domains of the 23S rRNA within the 50S subunit and the ribosome. The protein’s globular domain is positioned near the polypeptide exit tunnel on the outer surface of the subunit, while an extended beta-hairpin structure lines the wall of the exit tunnel at the center of the 70S ribosome, contributing to its structural integrity.