Analytical Data
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Gene name
RPL3L
- Application
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Alternative Names
60S ribosomal protein L3-like; Ribosomal protein L3 like; RL3L_HUMAN; RPL3L
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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
Q92901
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Expression Region
1-407 aa
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AA Sequence
MSHRKFSAPR HGHLGFLPHK RSHRHRGKVK TWPRDDPSQP VHLTAFLGYK AGMTHTLREV HRPGLKISKR EEVEAVTIVE TPPLVVVGVV GYVATPRGLR SFKTIFAEHL SDECRRRFYK DWHKSKKKAF TKACKRWRDT DGKKQLQKDF AAMKKYCKVI RVIVHTQMKL LPFRQKKAHI MEIQLNGGTV AEKVAWAQAR LEKQVPVHSV FSQSEVIDVI AVTKGRGVKG VTSRWHTKKL PRKTHKGLRK VACIGAWHPA RVGCSIARAG QKGYHHRTEL NKKIFRIGRG PHMEDGKLVK NNASTSYDVT AKSITPLGGF PHYGEVNNDF VMLKGCIAGT KKRVITLRKS LLVHHSRQAV ENIELKFIDT TSKFGHGRFQ TAQEKRAFMG PQKKHLEKET PETSGDL
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Molecular Weight
46.2 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
RPL3L, a member of the ribosomal protein family, plays a crucial role in the assembly and function of the ribosome, the cellular machinery responsible for protein synthesis. Research has shown that RPL3L is involved in various biological processes, including growth, development, and the regulation of cell cycle progression. Alterations in the expression or function of RPL3L have been linked to several diseases, particularly cancers, making it an important target for therapeutic intervention. In the context of ribosomal biogenesis, RPL3L is essential for the proper translation of mRNAs, directly influencing cellular homeostasis. Investigating RPL3L as a recombinant protein offers insights into its structural and functional properties, enabling researchers to elucidate its specific role in ribosome assembly and its impact on cellular functions under normal and pathological conditions. This line of research may facilitate the development of novel strategies for targeting ribosomal dysregulation in cancer and other diseases, potentially leading to innovative therapeutic approaches. As a result, the study of RPL3L not only advances our understanding of ribosome biology but also opens avenues for clinical applications in cancer therapy and beyond.











