Analytical Data
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Gene name
EEF1D
- Application
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Alternative Names
EEF1D；EF1D;Elongation factor 1-delta
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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
P29692
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Expression Region
1-281aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMATNFLAHEKIWFDKFKYDDAERRFYEQMN GPVAGASRQENGASVILRDIARARENIQKSLAGSSGPGASSGTSGDHGEL VVRIASLEVENQSLRGVVQELQQAISKLEARLNVLEKSSPGHRATAPQTQ HVSPMRQVEPPAKKPATPAEDDEDDDIDLFGSDNEEEDKEAAQLREERLR QYAEKKAKKPALVAKSSILLDVKPWDDETDMAQLEACVRSIQLDGLVWGA SKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFNK I
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Molecular Weight
33 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
EEF1D, or eukaryotic translation elongation factor 1 delta, is a crucial protein involved in the translation process of eukaryotic cells, playing a pivotal role in the elongation phase of mRNA translation. Research has indicated that EEF1D is not only essential for protein synthesis but is also linked to several cellular processes, including cell proliferation, apoptosis, and stress responses. Its involvement in the regulation of the translation machinery makes it a point of interest in various pathological conditions, including cancer, where dysregulation of protein synthesis is common. Recent studies have suggested that EEF1D may have additional roles beyond its canonical function, contributing to cellular signaling pathways and possibly influencing the tumor microenvironment. The recombinant expression of EEF1D has been pursued to better understand its structure-function relationships and interactions with other cellular components. This research seeks to elucidate the potential of EEF1D as a therapeutic target, providing insights into its mechanistic roles and possibilities for intervention in diseases characterized by altered protein synthesis. Understanding the dynamics of EEF1D through recombinant protein studies could pave the way for novel strategies in drug development and therapeutic applications, highlighting its relevance in both fundamental biology and clinical settings.
