Analytical Data
-
Gene name
SNUPN1
- Application
-
Alternative Names
SNUPN1；Snurportin-1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O95149
-
Expression Region
1-360aa
-
AA Sequence
MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS PDHPGCLMEN
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SNUPN1, also known as Small Nuclear Ubiquitin-like Modifier (SUMO) Protein 1, plays a pivotal role in cellular processes, including gene expression regulation, DNA repair, and the response to stress. As a key component of the SUMOylation pathway, SNUPN1 is involved in the post-translational modification of various target proteins, influencing their stability, localization, and activity. Research has increasingly focused on elucidating the functional mechanisms of SNUPN1, particularly in relation to its implications in cancer biology and neurodegenerative diseases. Given its significance in modifying transcription factors and other regulatory proteins, alterations in SNUPN1 activity could lead to disrupted cellular homeostasis and contribute to tumorigenesis or neuronal dysfunction. Recent studies have also explored the potential of targeting SNUPN1 in therapeutic strategies, aiming to modulate SUMOylation processes for improved disease outcomes. Understanding the structural properties and interaction networks of SNUPN1 is crucial for developing innovative approaches for intervention in diseases where SUMOylation is dysregulated. This ongoing research highlights the importance of SNUPN1 not only as a fundamental component of cellular regulatory mechanisms but also as a promising target for future pharmacological interventions.
