Analytical Data
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Gene name
CLEC14A
- Application
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Alternative Names
CLEC14A；C14orf27；EGFR5；C-type lectin domain family 14 member A
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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
Q86T13
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Expression Region
22-398aa
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AA Sequence
MASMTGGQQMGRGHHHHHHENLYFQGGEFEHPTADRAGCSASGACYSLHH ATMKRQAAEEACILRGGALSTVRAGAELRAVLALLRAGPGPGGGSKDLLF WVALERRRSHCTLENEPLRGFSWLSSDPGGLESDTLQWVEEPQRSCTARR CAVLQATGGVEPAGWKEMRCHLRANGYLCKYQFEVLCPAPRPGAASNLSY RAPFQLHSAALDFSPPGTEVSALCRGQLPISVTCIADEIGARWDKLSGDV LCPCPGRYLRAGKCAELPNCLDDLGGFACECATGFELGKDGRSCVTSGEG QPTLGGTGVPTRRPPATATSPVPQRTWPIRVDEKLGETPLVPEQDNSVTS IPEIPRWGSQS
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Molecular Weight
43 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 is a member of the C-type lectin-like domain family, known for its role in various biological processes, including immune responses, angiogenesis, and cell adhesion. Recent studies have highlighted its significant involvement in cancer biology, particularly in tumor progression and metastasis. The overexpression of CLEC14A has been observed in various malignancies, suggesting its potential as a biomarker for cancer diagnosis and prognosis. Moreover, the specific binding properties of CLEC14A to glycosylated proteins open avenues for therapeutic targeting in cancer treatment. The production of CLEC14A as a recombinant protein has gained momentum, allowing researchers to investigate its functional roles and mechanisms in cellular interactions and signaling pathways. Utilizing advanced techniques such as CRISPR-Cas9 gene editing and various purification methods, scientists aim to elucidate the precise biological functions of CLEC14A and its interactions with other cellular components. Understanding the molecular mechanisms underlying CLEC14A's involvement in tumor biology may provide insights into new therapeutic strategies and enhance our knowledge of cancer pathology, thereby contributing to the development of more targeted and effective cancer treatments. Furthermore, the study of CLEC14A also opens up potential research avenues in related fields, such as immunotherapy and regenerative medicine, where its properties may be harnessed for innovative approaches to treatment. As research continues to advance, CLEC14A remains a promising target that could lead to significant breakthroughs in cancer therapy and overall patient outcomes.
