Analytical Data
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Gene name
BCAN
- Application
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Alternative Names
BEHAB; CSPG7; Chondroitin Sulfate Proteoglycan 7; Brevican Proteoglycan; Brevican core protein; Brain-enriched hyaluronan-binding protein
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Species
Mouse
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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 SDS-PAGE.
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Uniprot
Q61361
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Expression Region
Asp23~Arg353
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Molecular Weight
43kDa
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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
BCAN, or Brevican, is a member of the link protein family, primarily found in the central nervous system and playing a critical role in the structure and functionality of the extracellular matrix in the brain. Research into BCAN recombinant proteins has gained attention due to their potential implications in understanding various neurological disorders, including traumatic brain injury, multiple sclerosis, and certain neurodegenerative diseases. The ability to produce BCAN in a recombinant form allows for in-depth studies of its biochemical properties and interactions with other matrix components, potentially leading to insights into neural repair mechanisms and synaptic functions. By elucidating the roles of BCAN in the extracellular matrix, researchers aim to develop targeted therapeutic strategies that can enhance recovery following neural injuries or mitigate the progression of neurodegenerative conditions. Current studies are focused on characterizing the structural and functional aspects of BCAN, evaluating its interactions with other proteins, and investigating its effects on neuronal health and plasticity. Furthermore, as the field of regenerative medicine evolves, BCAN recombinant proteins may serve as crucial tools for developing novel biomaterials to support neural tissue engineering and promote repair in damaged neural environments. Overall, the study of BCAN recombinant proteins represents a vital area of research with the potential to advance our understanding of brain homeostasis and pathology, driving forward therapeutic innovations for neurological health.
