Analytical Data
-
Gene name
NPL
- Application
-
Alternative Names
NPL;C1orf13;N-acetylneuraminate lyase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BXD5
-
Expression Region
1-320aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMAFPKKKLQGLVAATITPMTENGEINFSVI GQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLDQ VIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKE VAAAAPALPFYYYHIPALTGVKIRAEELLDGILDKIPTFQGLKFSDTDLL DFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQM LEAFEQKDFSLALNYQFCIQRFINFVVKLGFGVSQTKAIMTLVSGIPMGP PRLPLQKASREFTDSAEAKLKSLDFLSFTDLKDGNLEAGS
-
Molecular Weight
37 kDa
-
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
Nuclear pore complexes (NPCs) are critical structures that facilitate the transport of molecules between the nucleus and the cytoplasm in eukaryotic cells. Among the various components of NPCs, nucleoporins (Nups) are integral proteins that play essential roles in maintaining the structural integrity of these complexes and regulating nucleocytoplasmic transport. Recent studies have focused on the role of Nup78 and Nup84 in the assembly and stability of the NPC, highlighting their importance in cellular homeostasis. Abnormalities in NPC function or nucleoporin expression can lead to various diseases, including cancer and neurodegenerative disorders. Therefore, understanding the structural dynamics and functional properties of nucleoporins is critical for elucidating the mechanisms underlying these conditions and developing targeted therapeutic strategies. Recent advancements in techniques such as cryo-electron tomography and single-particle tracking have provided unprecedented insights into the modular organization of nucleoporins and their interactions within the NPC. These findings have opened new avenues for research into the regulatory mechanisms of nucleocytoplasmic transport and the potential for therapeutic interventions in diseases linked to nucleoporin dysfunction. As a result, ongoing investigations into the assembly and function of NPL (Nucleoporins and their associated proteins) continue to be a vibrant area of molecular and cellular biology, with implications for understanding fundamental cellular processes and their dysregulation in disease.
