Analytical Data
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Gene name
GPA33
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简介
The GPA33 protein may play a role in fundamental cellular processes, particularly in intercellular recognition and signaling, suggesting its involvement in intercellular communication. The exact mechanism by which GPA33 functions in these processes remains an area of interest, emphasizing its potential importance in mediating molecular interactions that contribute to cellular responses. GPA33 Protein, Human (HEK293, Fc) is the recombinant human-derived GPA33 protein, expressed by HEK293, with C-hFc labeled tag.
- Application
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Alternative Names
Cell Surface A33 Antigen; Glycoprotein A33; GPA33
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Species
Human
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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
Q99795
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Expression Region
I22-V235
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Molecular Weight
60-65 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
GPA33, a glycoprotein predominantly expressed on the surface of cancer cells, particularly in colorectal cancer, has emerged as a promising target for therapeutic interventions. Its unique expression profile, being minimally present in normal tissues, suggests potential for specificity in cancer treatment. The interest in GPA33 is driven by its involvement in tumor progression and metastasis, making it a valuable biomarker for diagnosis and prognosis. Recent studies have focused on the development of GPA33-targeted therapies, including monoclonal antibodies and chimeric antigen receptor (CAR) T-cell therapies, aimed at enhancing the immune response against GPA33-positive tumors. The challenges associated with the design of effective GPA33-targeted therapies include the need for precise identification of GPA33 expression levels in various tumor types and the minimization of off-target effects. Ongoing research is also exploring the potential of GPA33 as a platform for targeted drug delivery systems, which could significantly improve therapeutic outcomes. Overall, the study of GPA33 and its recombinant proteins represents a critical step toward innovative cancer treatments, with implications for improving patient survival and quality of life in colorectal cancer and potentially other malignancies. Continued exploration of GPA33’s biological functions and interactions within the tumor microenvironment is essential for harnessing its full potential in precision oncology.
