Analytical Data
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Gene name
AGR2
- Application
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Alternative Names
AGR2；AG2；Anterior gradient Protein 2 homolog
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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
O95994
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Expression Region
21-175aa
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AA Sequence
RDTTVKPGAK KDTKDSRPKL PQTLSRGWGD QLIWTQTYEE ALYKSKTSNK PLMIIHHLDE CPHSQALKKV FAENKEIQKL AEQFVLLNLV YETTDKHLSP DGQYVPRIMF VDPSLTVRAD ITGRYSNRLY AYEPADTALL LDNMKKALKL LKTEL
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Molecular Weight
22 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
AGR2 (anterior gradient 2) is a member of the anterior gradient family of proteins and has garnered significant interest in recent years due to its role in various biological processes and disease states, particularly in cancer. Initially identified as a protein involved in embryonic development and organogenesis, AGR2 has been linked to the regulation of epithelial cell homeostasis and differentiation. Its overexpression has been observed in various malignancies, including breast and lung cancers, correlating with aggressive tumor characteristics and poor prognostic outcomes. Given its potential as a biomarker and therapeutic target, researchers are increasingly focusing on the structural and functional analysis of recombinant AGR2 protein. The ability to produce recombinant AGR2 allows for the elucidation of its biological functions, interaction partners, and mechanisms of action at a molecular level. Additionally, understanding its molecular structure can inform potential drug design strategies aimed at inhibiting its function in cancer progression. The investigation of AGR2's role in cellular stress responses, protein folding, and secretion further emphasizes its significance in pathophysiology. Overall, the research on recombinant AGR2 protein provides a foundation for novel diagnostic and therapeutic approaches in cancer treatment, highlighting the need for continued exploration of its biological implications and clinical relevance.
