Analytical Data
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Gene name
SEC22L2
- Application
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Alternative Names
SEC22A; SEC22L2; Vesicle-trafficking protein SEC22a; SEC22 vesicle-trafficking protein homolog A; SEC22 vesicle-trafficking protein-like 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96IW7
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Expression Region
1-307 aa
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AA Sequence
MSMILSASVIRVRDGLPLSASTDYEQSTGMQECRKYFKMLSRKLAQLPDRCTLKTGHYNINFISSLGVSYMMLCTENYPNVLAFSFLDELQKEFITTYNMMKTNTAVRPYCFIEFDNFIQRTKQRYNNPRSLSTKINLSDMQTEIKLRPPYQISMCELGSANGVTSAFSVDCKGAGKISSAHQRLEPATLSGIVGFILSLLCGALNLIRGFHAIESLLQSDGDDFNYIIAFFLGTAACLYQCYLLVYYTGWRNVKSFLTFGLICLCNMYLYELRNLWQLFFHVTVGAFVTLQIWLRQAQGKAPDYDV
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Molecular Weight
59.51 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
SEC22L2, a member of the SEC22 family of proteins, plays a crucial role in the secretory pathway of eukaryotic cells, particularly involved in the transport of proteins between the endoplasmic reticulum (ER) and the Golgi apparatus. Its significance has been highlighted in numerous studies focusing on cellular mechanisms such as membrane trafficking, protein sorting, and secretion processes. Dysregulation of SEC22L2 has been implicated in various diseases, including metabolic disorders and certain cancers, indicating its potential as a therapeutic target. Recent research has explored the structural and functional characteristics of SEC22L2, revealing its role in vesicle formation and fusion, as well as its interactions with other cellular proteins involved in the trafficking process. Understanding the molecular mechanisms underlying SEC22L2’s function may provide insights into the pathology of diseases and could open new avenues for developing targeted therapies that modulate its activity. Continued investigation into SEC22L2 is essential to elucidate its contributions to cellular functions, its involvement in disease, and its potential roles in biotechnological applications.











