Analytical Data
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Gene name
CHL1
- Application
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Alternative Names
Neural cell adhesion molecule L1-like protein; CHL1; CALL
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Species
Human
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00533-1
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Expression Region
I25-Q1080
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Protein Length
Partial
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Molecular Weight
160-180 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
Related Products
Protein Description
CHL1, or Cell Adhesion Molecule L1, is a member of the immunoglobulin superfamily that plays a critical role in neuronal development and plasticity. It is primarily expressed in the nervous system and is involved in various processes such as axon guidance, neuronal migration, and regeneration. Dysregulation of CHL1 has been linked to several neurodegenerative diseases and psychiatric disorders, making it a significant target for research. The study of recombinant CHL1 protein is essential for understanding its functional mechanisms and the molecular pathways it influences. By producing this protein in a controlled laboratory environment, researchers can investigate the structure-function relationship, analyze CHL1's interactions with other proteins, and explore its potential as a therapeutic target. Furthermore, recombinant CHL1 can be utilized in various assays, including cell adhesion and migration studies, to elucidate its role in cell signaling and communication. This research contributes to a deeper understanding of neuronal development and holds promise for developing strategies to address neurological disorders linked to CHL1 dysfunction.
