Analytical Data
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Gene name
TROP-2
- Application
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Alternative Names
Tumor-associated calcium signal transducer 2; Tacstd2; Trop2; Cell surface glycoprotein Trop-2
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Species
Mouse
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Source
HEK293
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Tag
C-Avi;C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8BGV3
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Expression Region
Q25-G270
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Molecular Weight
75-90 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
Related Products
Protein Description
TROP-2, a transmembrane glycoprotein, has emerged as a significant target in cancer research due to its overexpression in various malignancies, including breast, lung, and colon cancers. Initially identified as an early developmental marker, TROP-2 plays a critical role in cellular adhesion and signaling pathways that promote tumor growth and metastasis. Its involvement in cancer progression has led to increased interest in developing TROP-2-targeted therapies, such as antibody-drug conjugates (ADCs) that deliver cytotoxic agents specifically to tumor cells expressing this protein. The unique expression pattern of TROP-2 in tumors, coupled with its limited presence in normal tissues, underscores its potential as a therapeutic target. Recent studies have focused on elucidating the molecular mechanisms by which TROP-2 contributes to oncogenesis and exploring its potential in combination therapies to enhance treatment efficacy. As a result, the development of TROP-2-targeted therapies is poised to improve outcomes for patients with TROP-2-positive cancers, making it a critical area of investigation in the quest for more effective cancer treatments.
