Analytical Data
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Gene name
ELP5
- Application
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Alternative Names
ELP5；C17orf81；DERP6;Elongator complex Protein 5
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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
Q8TE02
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Expression Region
1-316aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTPSEGA RAGTGRELEM LDSLLALGGL VLLRDSVEWE GRSLLKALVK KSALCGEQVH ILGCEVSEEE FREGFDSDIN NRLVYHDFFR DPLNWSKTEE AFPGGPLGAL RAMCKRTDPV PVTIALDSLS WLLLRLPCTT LCQVLHAVSH QDSCPGDSSS VGKVSVLGLL HEELHGPGPV GALSSLAQTE VTLGGTMGQA SAHILCRRPR QRPTDQTQWF SILPDFSLDL QEGPSVESQP YSDPHIPPVD PTTHLTFNLH LSKKEREARD SLILPFQFSS EKQQALLRPR PGQATSHIFY EPDAYDDLDQ EDPDDDLDI
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Molecular Weight
37 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
ELP5, a crucial component of the Elongator complex, plays a significant role in the modification of tRNAs and the regulation of transcription. Its relevance has intensified with the recognition of its involvement in various cellular processes, including gene expression and stress responses. Given that alterations in ELP5 function are associated with several diseases, including cancer and neurodegenerative disorders, researchers have focused on understanding its molecular mechanisms and interactions. The study of ELP5 recombinant proteins has emerged as a vital approach to investigate its structural features and functional roles. By producing ELP5 in a recombinant form, scientists can analyze its biochemical properties, elucidate its interactions with other cellular components, and assess its enzymatic activities. This research not only enhances our understanding of ELP5's role in cellular physiology but also provides insights into its potential as a therapeutic target. Understanding the structure-function relationship of ELP5 may lead to novel strategies for manipulating its activity in disease contexts, thereby underscoring its significance in both fundamental biology and clinical applications.
