Analytical Data
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Gene name
trhO
- Application
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Alternative Names
trhO；C9orf97；Thiosulfate sulfurtransferase/rhodanese-like domain-containing Protein 2
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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
Q252M0
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Expression Region
1-325aa
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AA Sequence
MKKNYYALAYYHFTRVDNPQEEIALHKELFKKLDVSCRIYISEQGINGQFSGYQPDAEYYMNWLKQRPGFSNVKFKIHHIEENIFPRATVKYRKELVALGCDVDLSNQGKHISPKEWHEKLEENRCLVLDVRNNYEWKIGHFENAVLPDIQTFREFPEYAEQLSKEHDPETTPVMMYCTGGIRCELYSSLLLEKGFKEVYQLDGGVIAYGQAMGTGKWRGKLFVFDDRLAVPIDEADTDVSPIAQCSHCEASCDTYYNCANTDCNNLFICCEECIHSTKGCCSQECSQAPRIRSFSTSRGNKPFRRMHLCEISEEQEKPLSCCLR
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Molecular Weight
43.6 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
TRH (thyrotropin-releasing hormone) is a tripeptide hormone synthesized in the hypothalamus that plays a critical role in the regulation of the hypothalamic-pituitary-thyroid axis. The exploration of TRH as a recombinant protein has gained traction in biomedical research due to its implications in various physiological processes, including metabolism, thermoregulation, and growth. TRH exerts its effects by stimulating the release of thyroid-stimulating hormone (TSH) from the anterior pituitary, which in turn promotes the synthesis and secretion of thyroid hormones from the thyroid gland. This intricate hormonal regulation is crucial for maintaining homeostasis in the body. Additionally, TRH has been implicated in modulating stress responses and influencing cognitive functions. The production of recombinant TRH has been facilitated by advancements in genetic engineering and protein expression systems, allowing for detailed studies on its structure-function relationships and potential therapeutic applications. Researchers are particularly interested in the potential of TRH in treating conditions such as hypothyroidism, depression, and obesity, where thyroid function and hormonal balance are disrupted. Moreover, the use of recombinant TRH in clinical studies could provide insights into its pharmacokinetics and pharmacodynamics, paving the way for the development of TRH-based therapeutic interventions. Overall, the investigation of TRH-recombinant proteins holds promise for enhancing our understanding of endocrine regulation and developing novel treatment strategies for various metabolic disorders.
