Recombinant Human 60S Ribosomal Protein L11 (RPL11) Protein (GST)

Name: Recombinant Human 60S Ribosomal Protein L11 (RPL11) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08541P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human 60S Ribosomal Protein L11 (RPL11) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P62913
Target Symbol	RPL11
Synonyms	60S ribosomal protein L11; Cell growth inhibiting protein 34; Cell growth inhibiting protein34; CLL associated antigen KW 12; CLL associated antigen KW12; CLL-associated antigen KW-12; DBA 7; DBA7; GIG 34; GIG34; L11; Ribosomal protein L11; RL11_HUMAN; RPL 11; Rpl11
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	QDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRRTGCIGAKHRISKEEAMRWFQQKYDGIILPGK
Expression Range	3-178aa
Protein Length	Partial
Mol. Weight	47.1kDa
Research Area	Cell Cycle
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. Promotes nucleolar location of PML.
Subcellular Location	Nucleus, nucleolus. Cytoplasm.
Protein Families	Universal ribosomal protein uL5 family
Database References	HGNC: 10301 OMIM: 604175 KEGG: hsa:6135 STRING: 9606.ENSP00000363676 UniGene: PMID: 27829214 A novel pathogenic mutation in RPL11 identified in a patient diagnosed with diamond Blackfan anemia as a young adult. PMID: 27667165 RPL splicing variant is associated with Diamond-Blackfan anemia. PMID: 28742285 Simulation of HEY1 Ser-68 phosphorylation prevents its interaction with p53, RPL11 and MDM2 and abolishes HEY1 migration to nucleolar caps upon ribosomal stress. Our findings uncover a novel mechanism for cross-talk between Notch signalling and nucleolar stress PMID: 27129302 Data suggest 5S ribosomal RNA is a direct target of miR-150 and miR-383 in esophageal squamous cell carcinoma (ESCC); overexpression of miR-150 and miR-383 inhibits ESCC cell proliferation in vitro and in vivo and intensifies RPL11/c-Myc interaction. PMID: 26606907 Data indicate that ribosomal protein (L11) promotes the recruitment of microRNA-130a (miR-130a) to oncoprotein c-Myc in response to UV irradiation treatment. PMID: 25544755 Data indicate that ribosomal protein L11 (RPL11)-expressing cells proliferated more rapidly than the ribosomal protein L11 (RPL11)-expressing cells. PMID: 25829192 levels of branched-chain aminotransferase-1 (BCAT1) transcripts are significantly decreased on the polysomes of both RPS19 and RPL11 cells and that translation of BCAT1 protein is especially impaired in cells with small RP gene mutations PMID: 24463277 Findings suggest that PICT1 has a crucial role in gastric cancer progression by regulating the MDM2-TP53 pathway through RPL11. PMID: 24045667 RPL11 mutations led to a dramatic decrease in progenitor cell proliferation and a delayed erythroid differentiation with a marked increase in apoptosis and G0/1 cell cycle arrest with activation of p53. PMID: 22833095 The studies provide insights on how nucleolar stress through L11 and NEDD8 can activate the transcriptional activity of p53. PMID: 22081073 ARF activates p53, at least partly by induction of ribosomal stress, which results in L11 suppression of MDM2 PMID: 22467867 Hydrophilic residues are crucial for ribosomal protein L11 (RPL11) interaction with zinc finger domain of MDM2 and p53 protein activation PMID: 21903592 Results identify a novel regulatory paradigm wherein L11 plays a critical role in controlling c-myc mRNA turnover via recruiting miR-24/miRISC in response to ribosomal stress. PMID: 21807902 Data report that depletion of L37 leads to cell cycle arrest in a MDM2/L11- and p53-dependent manner. PMID: 20935493 L11 suppresses c-Myc-dependent and RNA polymerase III-catalyzed transcription of 5 S rRNA and tRNA genes in response to ribosomal stress, ensuring a tight coordination between c-Myc activity and ribosomal biogenesis. PMID: 20194507 cells survey the maturation of the small and large ribosomal subunits by separate molecular routes, which may merge in an L11-dependent signaling pathway for p53 stabilization. PMID: 20056613 L11 functions as a negative regulator of HDM2 and there might exist in vivo an L11-HDM2-p53 pathway for monitoring ribosomal integrity PMID: 14612427 L11 is not regulated by transcription or protein stability and its level remains relatively constant during serum starvation, which induces translocation of L11 from the nucleolus to the nucleoplasm, where it participates in a complex with HDM2 PMID: 15152193 differentially regulates the levels of ubiquitinated p53 and MDM2 and inhibits the turnover and activity of MDM2 through a post-ubiquitination mechanism PMID: 16803902 These results identify L11 as a feedback inhibitor of c-Myc and suggest a novel role for L11 in regulating c-Myc-enhanced ribosomal biogenesis. PMID: 17599065 Transcription factor YY1 participates in activation transcription of the human ribosomal protein L11 gene PMID: 18389627 RPL11 mutations are associated with abnormal thumbs in Diamond-Blackfan anemia patients. PMID: 19061985 Mutations in RPL11 were identified in two patients from 2 out of 28 families (7.1%). PMID: 19191325 The cell selectively upregulates the translation of mRNAs with a polypyrimidine tract at their 5'-transcriptional start site (5'-TOP mRNAs), including that encoding rpL11, on impairment of 40S ribosome biogenesis. PMID: 19287375 identify NEDD8 as a crucial regulator of L11 RP signalling to p53. A decrease in L11 NEDDylation during nucleolar stress causes relocalization of L11 from the nucleolus to the nucleoplasm. PMID: 19713960

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.