Analytical Data
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Gene name
FACA
- Application
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Alternative Names
FACA；FAA；FACA；FANCH；Fanconi anemia group A Protein
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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
O15360
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Expression Region
1-297aa
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AA Sequence
MSDSWVPRSASGQDPGGRRRAWAELLAGRVKREKYNPERAQKLKESAVRL LRSHQDLNALLLEVEGPLCKKLSLSKVIDCDSSEAYANHSSSFIGSALQD QASRLGVPVGILSAGMVASSVGQICTAPAETSHPVLLTVEQRKKLSSLLE FARYLLAHSMFSRLSFCQELWKIQSSLLLEAVWHLHVQGIVSLQELLESH PDMHAVGSWLFRNLCCLCEQMEASCQHADVARAMLSDFVQMFVLRGFQKN SDLRRTVEPEKMPQVAVDVLQRMLIFALDALAAGVQEESSTHKIVRC
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Molecular Weight
58 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
FACA (Follistatin-related protein) is a crucial protein involved in various biological processes, including muscle development, cell signaling, and tissue repair. Research on FACA recombinant proteins has gained significant traction due to their potential therapeutic applications in regenerative medicine and disease treatment. Understanding the structure and function of FACA is essential for elucidating its role in modulating biological pathways, particularly in muscle atrophy and fibrosis-related conditions. The development of recombinant FACA proteins allows for detailed studies on its mechanisms of action and interactions with other signaling molecules, which can pave the way for novel therapeutic strategies. Furthermore, exploring the potential of FACA in muscle regeneration and repair can provide insights into combating age-related muscle loss and other degenerative diseases. The ongoing advancements in recombinant protein technology have made it possible to produce high yields of functional FACA, facilitating extensive biomedical research and applications in drug development and gene therapy.
