Analytical Data
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Gene name
NEURL2
- Application
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Alternative Names
NEURL2;C20orf163;Neuralized-like Protein 2
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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
Q9BR09
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Expression Region
1-285aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAAASEPVDSGALWGLERPEPPPTRFH RVHGANIRVDPSGTRATRVESFAHGVCFSREPLAPGQVFLVEIEEKELGW CGHLRLGLTALDPASLAPVPEFSLPDLVNLGHTWVFAITRHHNRVPREGR PEAEAAAPSRPPTLLVEPYLRIEQFRIPRDRLVGRSRPGLYSHLLDQLYE LNVLPPTARRSRLGVLFCPRPDGTADMHIIINGEDMGPSARGLPAAQPLY AVVDVFASTKSVRLVQLEYGLPSLQTLCRLVIQRSMVHRLAIDGLHLPKE LKDFCKYE
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Molecular Weight
34 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
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Protein Description
NEURL2 (Neural Renin-angiotensin System Component 2) is a gene that encodes a member of the E3 ubiquitin ligase family, which plays a crucial role in protein degradation and regulation of various cellular processes. Its involvement in neural development and potential link to neurodegenerative diseases has garnered increasing attention from researchers. Studies suggest that NEURL2 may influence neuronal survival, synaptic function, and response to stress, making it a significant candidate for understanding the underlying mechanisms of neurodegenerative disorders like Alzheimer's and Parkinson's disease. Given its role in ubiquitination, NEURL2 might contribute to the maintenance of protein homeostasis in neurons, and its dysregulation could lead to the accumulation of misfolded proteins, a hallmark of many neurodegenerative conditions. Current research efforts are focused on characterizing the structure and function of NEURL2 recombinant proteins, exploring their interactions with other cellular proteins, and elucidating their roles in neuronal stress response pathways. Understanding NEURL2 through recombinant protein studies can provide insights into its potential as a therapeutic target and enhance our knowledge of the molecular pathology of neurodegeneration. Overall, the investigation of NEURL2 holds promise for unveiling novel strategies aimed at mitigating the effects of neurodegenerative diseases and improving neurological health.











