Analytical Data
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Gene name
CLTA
- Application
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Alternative Names
CLTA;Clathrin light chain A
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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
P09496
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Expression Region
1-218aa
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AA Sequence
MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGPQPHGEPPGGPDAVDGVMNGEYYQESNGPTDSYAAISQVDRLQSEPESIRKWREEQMERLEALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNRAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH
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Molecular Weight
50.7kDa
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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
CLTA (Clathrin-AP180-CLIP-Associated Protein) is a crucial protein involved in the endocytic pathway, playing a significant role in the clathrin-mediated endocytosis process essential for cellular uptake of nutrients and signaling molecules. Its function is primarily linked to the formation and stabilization of clathrin-coated vesicles, which are vital for intracellular transport. Research on CLTA has gained momentum due to its implications in various physiological processes and its potential association with diseases such as cancer and neurodegenerative disorders. Understanding the structural and functional characteristics of CLTA, especially through recombinant protein studies, offers insights into its mechanistic roles in cellular trafficking and vesicle dynamics. Furthermore, recombinant CLTA proteins serve as valuable tools for exploring protein-protein interactions and identifying potential biomarkers for diseases. Recent advancements in protein engineering and expression systems have enhanced the production of functional CLTA, paving the way for detailed functional assays and structural analyses. Enhanced knowledge of CLTA could inform therapeutic strategies targeting endocytic pathways, potentially contributing to the development of innovative treatments for diseases linked to dysregulated protein trafficking.
