Analytical Data
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Gene name
Ferritin heavy chain/FTH1
- Application
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Alternative Names
Cysteine-rich protein TTG-1LIM domain only protein 1 ;LMO-1T-cell translocation protein 1
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02794
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Expression Region
2-183aa
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Molecular Weight
48.1 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
Ferritin heavy chain (FTH1) is a crucial protein involved in iron storage and homeostasis within the body. It plays a significant role in many physiological processes, including cellular iron regulation, antioxidant defense, and modulation of immune responses. Abnormalities in FTH1 expression and function are associated with various diseases, such as neurodegenerative disorders, cancer, and cardiovascular diseases. With the increasing prevalence of iron-related disorders, understanding the mechanisms underlying FTH1 functionality has become a pertinent area of research. Recombinant FTH1 proteins are being developed for various applications, including therapeutic interventions and diagnostic tools. These recombinant proteins can be used to study the structure-function relationships of FTH1, investigate its role in iron metabolism, and explore potential therapeutic targets for disease treatment. Moreover, the generation of FTH1 recombinant proteins allows for the exploration of their properties in vitro and in vivo, providing insights into their clinical relevance. As research advances, recombinant FTH1 may offer novel approaches for managing conditions related to iron dysregulation and present opportunities to enhance our understanding of cellular iron dynamics.
