Recombinant Human 60S Ribosomal Protein L5 (RPL5) Protein (GST)

Name: Recombinant Human 60S Ribosomal Protein L5 (RPL5) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08486P
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 L5 (RPL5) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P46777
Target Symbol	RPL5
Synonyms	60S ribosomal protein L5; DBA6; L5; MSTP030; PPP1R135; protein phosphatase 1, regulatory subunit 135; Ribosomal protein L5; RL5; RL5_HUMAN; RP L5; RPL 5; RPL5; U21 RNA; U21RNA
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	GFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVTGDEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYIKNSVTPDMMEEMYKKAHAAIRENPVYEKKPKKEVKKKRWNRPKMSLAQKKDRVAQKKASFLRAQERAAES
Expression Range	2-297aa
Protein Length	Full Length of Mature Protein
Mol. Weight	61.2kDa
Research Area	Epigenetics And Nuclear Signaling
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.
Subcellular Location	Cytoplasm. Nucleus, nucleolus.
Protein Families	Universal ribosomal protein uL18 family
Database References	HGNC: 10360 OMIM: 603634 KEGG: hsa:6125 STRING: 9606.ENSP00000359345 UniGene: PMID: 28428269 Whole exome sequencing in the differential diagnosis of Diamond-Blackfan anemia: Clinical and molecular study of three patients with novel RPL5 and mosaic RPS19 mutations PMID: 28376382 Low RPL5 expression is associated with cancer. PMID: 28147343 Ribosomal proteins L11 and L5 activate TAp73 by overcoming MDM2 inhibition. PMID: 25301064 RPL5 mutation is associated with Diamond Blackfan Anemia. PMID: 25132370 Findings uncover a mechanism by which RPL5 and RPL11 can co-operatively suppress c-Myc expression, allowing a tightly controlled ribosome biogenesis in cells. PMID: 24141778 Unlike other tumor suppressors, RPL5 and RPL11 play essential roles in normal cell proliferation. PMID: 24061479 High frequency of RPL5 gene deletion is associated with Italian Diamond-Blackfan anemia. PMID: 22689679 Oncogenic splicing factor SRSF1 stabilizes the tumor suppressor protein p53 via RPL5, inducing cell senescence. PMID: 23478443 Mutations affect the ribosomal proteins RPL5 and RPL10 in 12 of 122 (9.8%) pediatric T-cell acute lymphoblastic leukemias. PMID: 23263491 disrupted nucleoli may provide a platform for L5- and L11-dependent p53 activation, implying a role for the nucleolus in p53 activation by ribosomal biogenesis stress PMID: 23169665 Data show 1 proband with an RPL5 deletion, 1 patient with an RPL35A deletion, 3 with RPS17 deletions, and 1 with an RPS19 deletion. PMID: 22262766 Data show that all patients with RPS19 and RPL5 mutations had physical abnormalities. PMID: 20378560 An analysis and fine mapping of GFI-EVI5-RPL5-FAM69A locus, genotyping eight Tag-single nucleotide polymorphisms in 732 multiple sclerosis patients and 974 controls from Spain, was performed. PMID: 20087403 Knockdown of L29 or L30 enhanced the interaction of MDM2 with L11 and L5 and markedly inhibited MDM2-mediated p53 ubiquitination, suggesting that direct perturbation of 60 S ribosomal biogenesis activates p53 via L11- and L5-mediated MDM2 suppression. PMID: 20554519 The study reports a high frequency of RPL5 (9.3%) and RPL11 (9.3%) mutations in a Diamond-Blackfan anemia cohort. PMID: 19773262 the presence of multiple NLSs in ribosomal protein L5 appears to allow for efficient nuclear transport via utilisation of multiple, mechanistically different import pathways. PMID: 11824785 the MDM2-L5-L11-L23 complex functions to inhibit MDM2-mediated p53 ubiquitination and thus activates p53 PMID: 15308643 interaction of NVL2 with L5 is ATP-dependent and likely contributes to the nucleolar translocation of NVL2 PMID: 15469983 Cancer-associated missense mutations targeting MDM2's central zinc finger disrupt the interaction of MDM2 with L5 and L11. PMID: 17116689 5-FU treatment triggers a ribosomal stress response so that ribosomal proteins L5, L11, and L23 are released from ribosome to activate p53 by ablating the MDM2-p53 feedback circuit PMID: 17242401 L11 cooperates with L5, resulting in a robust inhibition of the E3 activity of MDM2, and a stabilization and activation of p53 approaching that achieved by p14(ARF). PMID: 18560357 Susceptibility gene for multiple sclerosis in Australians. PMID: 18650830 RPL5 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients. PMID: 19061985 Mutations in RPL5 were identified in eight patients from 6 out of 28 families (21.4%). PMID: 19191325

FAQs

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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.