Analytical Data
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Gene name
RPL13A
- Application
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Alternative Names
RPL13A；Large ribosomal subunit Protein uL13
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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
P40429
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Expression Region
2-203aa
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AA Sequence
AEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ AEKNVEKKID KYTEVLKTHG LLV
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Molecular Weight
23.5 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
Related Products
Protein Description
RPL13A, a member of the ribosomal protein family, plays a crucial role in the assembly and function of the ribosome, which is essential for protein synthesis in all living cells. Research into RPL13A has gained significant attention due to its involvement in various cellular processes, including cell growth, proliferation, and stress responses. Dysregulation of RPL13A expression has been implicated in several human diseases, particularly cancer, where altered ribosomal biogenesis can contribute to malignant transformations. Recent studies have focused on characterizing RPL13A's structure and function, as well as its interaction with other ribosomal proteins and RNA, to understand its precise role in ribosome assembly and function. Moreover, the exploration of RPL13A as a potential biomarker for cancer prognosis and a target for therapeutic intervention has emerged as a promising avenue for future research. By generating recombinant RPL13A proteins, scientists aim to elucidate its molecular mechanisms, which could lead to novel strategies for treating diseases associated with ribosomal dysfunction. This underscores the importance of RPL13A in the larger context of molecular biology and its relevance in the field of biomedical research.
