Analytical Data
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Gene name
mTSH
- Application
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Species
Mouse
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01216 (L25-S120)&P12656
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Expression Region
P01216 (L25-S120)&P12656 (F21-V138)
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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
The research on recombinant mTSH (mouse Thyroid-Stimulating Hormone) has garnered significant attention in the field of endocrinology due to its crucial role in regulating thyroid function and overall metabolic processes. TSH, a glycoprotein hormone produced by the anterior pituitary gland, stimulates the thyroid gland to secrete thyroid hormones (T3 and T4), which are essential for maintaining metabolic homeostasis. Understanding the molecular structure and biological activity of mTSH is critical for elucidating its signaling pathways, potential receptor interactions, and the physiological consequences of TSH signaling dysregulation. With advances in recombinant DNA technology, scientists can now produce mTSH in vitro, allowing for detailed studies of its pharmacokinetics, receptor binding affinity, and bioactivity. This research holds promise for developing therapeutic strategies for thyroid disorders such as hypothyroidism and hyperthyroidism. Additionally, understanding mTSH's interactions with its receptor can provide insights into developing TSH analogs or antagonists, potentially leading to novel treatments for patients with thyroid-related diseases. Moreover, the study of mTSH can enhance our understanding of endocrine system dynamics and may shed light on broader metabolic syndromes, thereby improving clinical outcomes in various endocrine disorders. Ultimately, the investigation into recombinant mTSH serves not only to deepen our understanding of thyroid physiology but also to contribute to medical advancements in endocrinology.
