Analytical Data
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Gene name
FAM96B
- Application
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Alternative Names
FAM96B；CIAB；FAM96B；MIP18；Cytosolic iron-sulfur assembly component 2B
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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
Q9Y3D0
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Expression Region
1-163aa
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AA Sequence
VGGGGVGGGLLENANPLIYQRSGERPVTAGEEDEQVPDSIDAREIFDLIRSINDPEHPLTLEELNVVEQVRVQVSDPESTVAVAFTPTIPHCSMATLIGLSIKVKLLRSLPQRFKMDVHITPGTHASEHAVNKQLADKERVAAALENTHLLEVVNQCLSARS
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Molecular Weight
44.5 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
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Protein Description
FAM96B, also known as family with sequence similarity 96 member B, is a protein of interest in molecular biology and cancer research due to its potential roles in cellular processes such as proliferation, differentiation, and apoptosis. Emerging studies have suggested that FAM96B may influence various signaling pathways and interact with other cellular proteins, making it a candidate for further investigation in the context of tumorigenesis. Its expression levels have been linked to certain cancers, indicating that alterations in FAM96B could play a critical role in cancer development and progression. The recombinant form of FAM96B offers a valuable tool for studying its biochemical properties, functional roles, and interactions in vitro and in vivo. Understanding the exact mechanisms by which FAM96B exerts its effects could lead to novel therapeutic strategies and biomarkers for cancer diagnosis and treatment. Researchers are focusing on characterizing the structural and functional aspects of this protein, utilizing techniques such as gene cloning, protein expression, and purification, along with various assays to evaluate its biological activities. This research is crucial for elucidating the role of FAM96B in human health and disease, paving the way for future studies that could harness its potential in targeted therapies.
