Analytical Data
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Gene name
CAPSL
- Application
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Alternative Names
CAPSL；Calcyphosin-like Protein
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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
Q8WWF8
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Expression Region
1-208aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL
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Molecular Weight
26 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
CAPSL (Calcium-activated protein with a fibronectin type III-like domain) is a protein that has garnered significant interest in recent years due to its potential roles in various cellular processes, including cell adhesion, signaling, and immune response regulation. Its unique structure, characterized by the presence of fibronectin type III-like domains, suggests that CAPSL may interact with other proteins and extracellular matrices, influencing cellular dynamics. Research has shown that CAPSL is involved in critical biological functions such as promoting cell migration and modulating inflammatory responses, making it a potentially valuable target for therapeutic interventions in diseases like cancer and autoimmune disorders. Despite these insights, the functional mechanisms and pathways associated with CAPSL remain underexplored, highlighting the need for further investigation. The recombinant expression of CAPSL proteins allows for the detailed study of their structure-function relationships and interactions in controlled environments. Such studies are essential for elucidating the biological significance of CAPSL and its potential applications in medical science, including drug development and regenerative medicine. Understanding CAPSL's role at the molecular level could provide new avenues for manipulating immune response and tissue remodeling, contributing to innovative therapeutic strategies.
