Analytical Data
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Gene name
L1CAM
- Application
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Alternative Names
CD171; L1-CAM; CAML1; HSAS; HSAS1; MASA; MIC5; N-CAML1; S10; SPG1; Antigen Identified By Monoclonal Antibody R1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by reducing SDS-PAGE.
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Uniprot
P32004
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Expression Region
Thr218~Gln423
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Molecular Weight
26kDa
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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
L1CAM (L1 Cell Adhesion Molecule) is a critical protein involved in various biological processes, including cell adhesion, neuronal development, and axon guidance. Its dysregulation is implicated in several neurological disorders and cancers, making it a significant focus of research. The recombinant expression of L1CAM allows for detailed studies of its structure, function, and interactions, overcoming the limitations posed by natural sources. By using techniques such as recombinant DNA technology, researchers can produce L1CAM in various host systems, enabling investigations into its biochemical properties and role in cell signaling. Additionally, recombinant L1CAM can be utilized in therapeutic applications, such as targeted drug delivery and immunotherapy, by leveraging its adhesion properties to enhance cellular interactions and targeting specificity. Understanding the functionality of L1CAM at the molecular level can provide insights into its potential as a biomarker or therapeutic target, thereby contributing to the development of innovative strategies for treating related diseases.
