Analytical Data
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Gene name
FMNL2
- Application
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Alternative Names
FMNL2; FHOD2; KIAA1902Formin-like protein 2; Formin homology 2 domain-containing protein 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96PY5
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Expression Region
1-178aa
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AA Sequence
MDLTKREYTMHDHNTLLKEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQDPKSPSHKSKRQQQELIAELRRRQVKDNRHVYEGKDGAIEDIITALKKNNITKFPNVHSRVRISSSTPVVEDTQS
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Molecular Weight
45.32 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
FMNL2 (Formin-Like 2) is a member of the formin protein family, which plays a crucial role in the regulation of the actin cytoskeleton and is implicated in various cellular processes such as cell migration, division, and differentiation. This protein is known to influence actin polymerization and has been linked to important biological functions in contexts like tissue development and immune response. Recent studies have highlighted its potential involvement in several diseases, including cancer metastasis and neurodegenerative disorders. The study of FMNL2 recombinant proteins has gained significance as researchers aim to elucidate its precise mechanisms of action and functional roles within the cell. Understanding FMNL2’s structure and interactions with other cellular components is essential for uncovering its biological significance and therapeutic potential. By generating recombinant FMNL2 proteins, scientists can explore its dynamics in cellular pathways and assess its efficacy in various models, paving the way for potential interventions in FMNL2-related diseases. This research is imperative to not only enhance our understanding of cellular mechanics but also to devise strategies targeting FMNL2 in disease contexts, thus contributing to the development of novel therapeutic approaches.











