Analytical Data
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Gene name
CLEC14A
- Application
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Alternative Names
C-type lectin domain family 14 member A; EGFR-5; C14orf27
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Species
Rat
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q642B4
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Expression Region
M1-T398
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AA Sequence
MRPALALCLLCPAFWPRPGNGEHPTADRAVCSVPGACYSLHHAAMKRRAAEEACSLRGGTLSTVQSGSELQAVLKLFRAGPGPGGGSKDLMFWVALERDRSQCTQEREPLRGFSWLYTDSEDSENRTLPWVEEPQLSCTVRKCAVLQATGGVEPAGWKEMRCQQRADGYLCKYQFEALCPAPRPGAASNLSFQAPFRLSSSALDFSPPGTEVSAMCPRDFSVSSICVQEETGARWDGLFPGSLLCPCSGRYLLAGKCVELADCLDYLGNFACECAVGFELGKDKRSCETKAEGQLTLEGTKLPTRNVSATPASPVTNKSWPGQVYDKPGEMPQVTGQDRIATSVPEILQWGTQSTLPTVQTSPQTKPKVTITPSGSMMPTLNFASSPPVSLTFDSSST
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Protein Length
Partial
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Molecular Weight
90-120 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
CLEC14A, a member of the C-type lectin-like domain family, has garnered increasing interest in scientific research due to its potential role in angiogenesis and immune regulation. Expressed predominantly in endothelial cells, CLEC14A is thought to be involved in the formation of new blood vessels, making it a target of investigation in cancer biology and regenerative medicine. Studies have shown that its expression is upregulated in various tumor types, suggesting a possible link between CLEC14A and tumor progression. Furthermore, understanding the mechanisms by which CLEC14A influences endothelial cell behavior could unveil new therapeutic strategies for diseases characterized by aberrant angiogenesis, such as cancer, diabetic retinopathy, and cardiovascular disorders. Recent advancements in recombinant protein technology have enabled the production of CLEC14A for detailed functional analyses, allowing researchers to explore its structure-function relationships and interactions with other cellular components. By studying the recombinant CLEC14A protein, scientists aim to elucidate its biological roles, paving the way for the development of novel anti-angiogenic therapies or diagnostic tools for cancer and other angiogenesis-related diseases. Overall, the multifaceted role of CLEC14A in endothelial function and its implications in pathology make it a significant focus of current biomedical research.
