Analytical Data
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Gene name
NUP35
- Application
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Alternative Names
NUP35；MP44；NUP53；Nucleoporin NUP35
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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
Q8NFH5
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Expression Region
1-326aa
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AA Sequence
MAAFAVEPQGPALGSEPMMLGSPTSPKPGVNAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVPAHKDKSGAPPVRSIYDDISSPGLGSTPLTSRRQPNISVMQSPLVGVTSTPGTGQSMFSPASIGQPRKTTLSPAQLDPFYTQGDSLTSEDHLDDSWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVKPCIDKSVMESSDRCALSSPSLAFTPPIKTLGTPTQPGSTPRISTMRPLATAYKASTSDYQVISDRQTPKKDESLVSKAMEYMFGW
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Molecular Weight
42.2 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
NUP35, also known as nucleoporin 35, is a critical component of the nuclear pore complex (NPC), which serves as the gateway for nucleocytoplasmic transport of molecules. Research into NUP35 has garnered attention due to its essential role in maintaining nuclear envelope integrity and regulating gene expression by controlling the exchange of proteins and RNA between the nucleus and cytoplasm. This protein is part of the larger family of nucleoporins, which collectively contribute to the structural framework and functional dynamics of the NPC. Abnormalities in NUP35 expression or function have been implicated in various diseases, including cancer and genetic disorders, highlighting its potential as a biomarker and therapeutic target. Recent advances in recombinant protein technology have facilitated the production of NUP35, enabling detailed structural and biochemical studies. These studies aim to elucidate NUP35's role within the NPC and its interactions with other nucleoporins and transport factors. Understanding the exact mechanisms by which NUP35 operates can provide valuable insights into the fundamental processes of cellular communication and transport, as well as the pathological consequences of its dysfunction. Thus, the research on recombinant NUP35 not only enhances our grasp of nuclear transport mechanisms but also opens avenues for developing innovative therapeutic strategies to address diseases associated with nucleocytoplasmic transport dysregulation.
