Analytical Data
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Gene name
NUP62
- Application
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Alternative Names
NUP62;Nuclear pore glycoProtein p62
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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
P37198
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Expression Region
2-522aa
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AA Sequence
SGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FD
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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
NUP62, a crucial component of the nuclear pore complex (NPC), plays a significant role in nucleocytoplasmic transport, which is vital for maintaining cellular homeostasis. Research on NUP62 has gained momentum due to its involvement in various cellular processes, including gene expression regulation, cell cycle progression, and response to cellular stress. Recent studies have highlighted its implications in human diseases, particularly in cancer, where aberrant NUP62 expression has been associated with tumor progression and metastasis. The reconstitution and characterization of NUP62 as a recombinant protein have become essential for understanding its mechanistic role in nucleocytoplasmic transport and its interactions with other nucleoporins and cellular factors. By producing NUP62 in a controlled environment, researchers can study its structural properties, functional dynamics, and interaction with importin and exportin proteins. Furthermore, recombinant NUP62 enables the exploration of potential therapeutic applications, aiming to modulate its function in diseased states. Overall, the study of NUP62 not only sheds light on the fundamental mechanisms of nucleocytoplasmic transport but also holds promise for novel insights into targeting this pathway for disease intervention.
