60S ribosomal protein L11 (RPL11), partial, human, recombinant

60S ribosomal protein L11 (RPL11), partial, human, recombinant
Item number Size Datasheet Manual SDS Delivery time Quantity Price
CSB-RP000654h.20 20 µg -

10 - 14 business days*

219.00€
CSB-RP000654h.100 100 µg -

10 - 14 business days*

392.00€
CSB-RP000654h.1 1 mg -

10 - 14 business days*

1,628.00€
 
Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 3-178aa. Protein Length:... more
Product information "60S ribosomal protein L11 (RPL11), partial, human, recombinant"
Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 3-178aa. Protein Length: Partial. Tag Info: N-terminal GST-tagged. Target Protein Sequence: QDQGEKENPM RELRIRKLCL NICVGESGDR LTRAAKVLEQ LTGQTPVFSK ARYTVRSFGI RRNEKIAVHC TVRGAKAEEI LEKGLKVREY ELRKNNFSDT GNFGFGIQEH IDLGIKYDPS IGIYGLDFYV VLGRPGFSIA DKKRRTGCIG AKHRISKEEA MRWFQQKYDG IILPGK. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. 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 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: 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. Relevance: Binds to 5S ribosomal RNA . Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML . Reference: Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients.Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., Meerpohl J.J., Atsidaftos E. , Lipton J.M., Gleizes P.-E., Beggs A.H.Am. J. Hum. Genet. 83:769-780(2008). Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs
Keywords: RPL11, 60S ribosomal protein L11, CLL-associated antigen KW-12, Large ribosomal subunit protein uL5, Recombinant Human 60S ribosomal protein L11 (RPL11), partial
Supplier: Cusabio
Supplier-Nr: RP000654h

Properties

Application: Activity not tested
Conjugate: No
Host: E.coli
Species reactivity: human
MW: 47.1 kD
Purity: >90% (SDS-PAGE)

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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