Analytical Data
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Gene name
RPL4
- Application
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Alternative Names
60S ribosomal protein L1; 60S ribosomal protein L4; L4; Ribosomal protein L4; RL4_HUMAN; rpl4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P36578
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Expression Region
2-427 aa
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AA Sequence
ACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VDKAAAAAAA LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK AAATKKPAPE KKPAEKKPTT EEKKPAA
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Molecular Weight
47.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
RPL4, a vital component of the ribosomal 60S subunit, has garnered significant attention in biomedical research due to its crucial role in ribosome biogenesis and protein synthesis. Abnormalities in RPL4 expression have been linked to various pathologies, including cancer, where it may influence cell proliferation and apoptosis. Recent studies indicate that RPL4 may also play a regulatory role in cellular stress responses and gene expression modulation, suggesting its involvement in tumorigenesis and response to chemotherapeutic agents. The recombinant production of RPL4 provides a valuable tool for elucidating its functional mechanisms and interactions within the ribosome and broader cellular context. By generating and characterizing RPL4 recombinant proteins, researchers aim to understand the molecular underpinnings of its role in ribosome assembly and function, as well as its potential implications in diseases. Investigations into RPL4's binding partners and post-translational modifications may uncover novel insights into its contributions to translational control and cellular adaptability, positioning RPL4 as a potential biomarker or therapeutic target in cancer and other disorders. As the field of ribosome biology continues to evolve, the study of RPL4, especially in recombinant forms, remains a promising avenue for discovering new strategies for treatment and developing a deeper understanding of cellular mechanisms underlying health and disease.
