Analytical Data
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Gene name
NUP43
- Application
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Alternative Names
NUP43Nucleoporin Nup43; Nup107-160 subcomplex subunit Nup43; p42
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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
Q8NFH3
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Expression Region
1-380 aa
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AA Sequence
MEEIYAKFVS QKISKTRWRP LPPGSLQTAE TFATGSWDNE ENYISLWSIG DFGNLDSDGG FEGDHQLLCD IRHHGDVMDL QFFDQERIVA ASSTGCVTVF LHHPNNQTLS VNQQWTTAHY HTGPGSPSYS SAPCTGVVCN NPEIVTVGED GRINLFRADH KEAVRTIDNA DSSTLHAVTF LRTPEILTVN SIGQLKIWDF RQQGNEPSQI LSLTGDRVPL HCVDRHPNQQ HVVATGGQDG MLSIWDVRQG TMPVSLLKAH EAEMWEVHFH PSNPEHLFTC SEDGSLWHWD ASTDVPEKSS LFHQGGRSST FLSHSISNQA NVHQSVISSW LSTDPAKDRI EITSLLPSRS LSVNTLDVLG PCLVCGTDAE AIYVTRHLFS
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Molecular Weight
42.1 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
NUP43 is a member of the nuclear pore complex (NPC) protein family, playing a crucial role in nucleocytoplasmic transport and maintaining nuclear envelope integrity. Research on NUP43 recombinant proteins has gained importance due to their involvement in essential cellular processes, such as gene expression regulation and signal transduction. Disruptions in NUP43 function have been implicated in various diseases, including cancer, highlighting the need for a better understanding of its biological roles and mechanisms. The study of NUP43 recombinant proteins allows researchers to investigate their structure-function relationships, interactions with other nucleoporins, and impact on nuclear transport pathways. Additionally, exploring NUP43 could provide insights into the molecular basis of nuclear transport disorders and aid in the identification of potential therapeutic targets. By employing techniques such as X-ray crystallography, nuclear magnetic resonance (NMR), and cryo-electron microscopy, researchers can elucidate the three-dimensional structures of NUP43 and its complexes, paving the way for developing strategies to modulate its activity in pathological conditions. Overall, NUP43 recombinant protein research advances our understanding of nuclear transport mechanisms, molecular pathogenesis, and potential interventions for diseases linked to nucleoporins.
