Analytical Data
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Gene name
EEF1A1
- Application
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Alternative Names
EEF1A1；EEF1A；EF1A；LENG7;Elongation factor 1-alpha 1
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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
P68104
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Expression Region
1-462aa
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AA Sequence
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK ITKSAQKAQK AK
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Molecular Weight
50 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
EEF1A1, or Eukaryotic Translation Elongation Factor 1 Alpha 1, is a crucial protein involved in protein synthesis, playing a vital role in the elongation phase of translation by facilitating the delivery of aminoacyl-tRNA to the ribosome. Beyond its fundamental role in cell biology, EEF1A1 has garnered significant attention for its implications in various diseases, including cancer and neurodegenerative disorders. Research has shown that EEF1A1 is often overexpressed in tumor cells, correlating with enhanced cell proliferation and survival, thus positioning it as a potential biomarker for cancer progression and a target for therapeutic intervention. Additionally, the protein’s involvement in cellular stress responses and its interactions with other cellular pathways underscore its multifunctional role in cellular homeostasis. Recent advances in recombinant protein technology have enabled the production of EEF1A1 in various expression systems, facilitating in-depth studies of its structure and function. Understanding the molecular mechanisms by which EEF1A1 operates can provide valuable insights into its contributions to cellular physiology and pathology, casting light on potential avenues for novel treatments for diseases associated with aberrant EEF1A1 activity. Thus, the study of EEF1A1 not only enhances our fundamental knowledge of translation and protein synthesis but also opens up new investigative avenues in disease research and therapeutic development.
