Analytical Data
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Gene name
THUMPD2
- Application
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Alternative Names
THUMPD2; C2orf8; THUMP domain-containing Protein 2
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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
Q9BTF0
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Expression Region
1-503 aa
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AA Sequence
MSEARGEPGS GPEAGARFFC TAGRGLEPFV MREVRARLAA TQVEYISGKV FFTTCSDLNM LKKLKSAERL FLLIKKQFPL IISSVSKGKI FNEMQRLINE DPGSWLNAIS IWKNLLELDA KKEKLSQRDD NQLKRKVGEN EIIAKKLKIE QMQKIEENRD CQLEKQIKEE TLEQRDFTTK SEKFQEEEFQ NDIEKAIDTH NQNDLTFRVS CRCSGTIGKA FTAQEVGKVI GIAIMKHFGW KADLRNPQLE IFIHLNDIYS VVGIPVFRVS LASRAYIKTA GLRSTIAWAM ASLADIKAGA FVLDPMCGLG TILLEAAKEW PDVYYVGADV SDSQLLGTWD NLKAAGLEDK IELLKISVIE LPLPSESVDI IISDIPFGKK FKLGKDIKSI LQEMERVLHV GGTIVLLLSE DHHRRLTDCK ESNIPFNSKD SHTDEPGIKK CLNPEEKTGA FKTASTSFEA SNHKFLDRMS PFGSLVPVEC YKVSLGKTDA FICKYKKSHS SGL
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Molecular Weight
56.4 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
THUMPD2, a member of the THUMP domain-containing protein family, has garnered attention in recent years due to its potential roles in various cellular processes, including RNA metabolism and mitochondrial function. Initial studies suggest that THUMPD2 is involved in the regulation of gene expression and may act as a critical player in the stress response pathways within cells. Its unique structure, featuring a conserved THUMP domain, indicates a possible interaction with RNA molecules, which could implicate THUMPD2 in RNA stability and processing. Emerging research highlights its significance in maintaining cellular integrity under stress conditions, making it a candidate for further investigation in the context of diseases characterized by dysregulated RNA metabolism, such as cancer and neurodegenerative disorders. The recombinant production of THUMPD2 allows for detailed biochemical and structural studies, aiding in the elucidation of its functions and potential regulatory mechanisms. Understanding the role of THUMPD2 is crucial for unraveling its contributions to cellular homeostasis and its implications in pathological states, positioning it as a promising target for therapeutic intervention in RNA-related diseases.
