Analytical Data
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Gene name
ftnA
- Application
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Alternative Names
ftnA；Adam1；Ftna；Disintegrin and metalloProteinase domain-containing Protein 1a
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Species
E.coli
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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
P52093
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Expression Region
1-167aa
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AA Sequence
MLSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAKKLIVFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKGKDHATFNFLQWYVSEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGIAKSRKS
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Molecular Weight
21.8 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
The study of the ftnA gene, which encodes for ferritin, a key protein involved in iron storage and homeostasis, has gained significant attention in the field of molecular biology and biochemistry. Ferritin plays a crucial role in cellular processes by sequestering excess iron, thereby preventing oxidative damage caused by free iron. In various organisms, including bacteria, plants, and animals, ftnA and its recombinant protein forms have been explored for their potential applications in biotechnology and medicine, such as in iron supplementation therapies and as a biomarker for diseases related to iron metabolism. The recombinant expression of ftnA allows researchers to produce ferritin in controlled laboratory settings, facilitating studies on its structure-function relationships and its role in iron-related disorders. Additionally, understanding the mechanisms by which ftnA operates can aid in the development of novel therapeutic strategies against conditions like anemia and hemochromatosis. Through advancements in genetic engineering and protein purification techniques, the functional characterization of ftnA-derived proteins has provided insights into their stability, efficacy, and potential as drug delivery systems. Thus, research on ftnA recombinant proteins not only enhances our understanding of fundamental biological processes but also holds promise for innovative applications in health and disease management.
