Analytical Data
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Gene name
FGF12
- Application
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Alternative Names
FGF12；FGF12B；FHF1;Fibroblast growth factor 12
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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
P61328
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Expression Region
1-181aa
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AA Sequence
MESKEPQLKGIVTRLFSQQGYFLQMHPDGTIDGTKDENSDYTLFNLIPVG LRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSST LYRQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVCMYREQS LHEIGEKQGRSRKSSGTPTMNGGKVVNQDST
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Molecular Weight
21 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
FGF12 (Fibroblast Growth Factor 12) is a member of the fibroblast growth factor family, which plays a critical role in various biological processes, including embryonic development, cell proliferation, and tissue repair. Research on FGF12 has gained attention due to its potential implications in the nervous system, particularly in influencing neuronal development and function. Studies suggest that FGF12 may be involved in modulating synaptic transmission and may have a protective role in neurodegenerative conditions. The exploration of recombinant FGF12 proteins is essential for understanding its biological functions and uncovering the molecular mechanisms behind its activity. By producing and characterizing recombinant FGF12, researchers aim to investigate its interactions with specific receptors and signaling pathways, which may shed light on its therapeutic potential for neurological disorders. The generation of these proteins allows for more detailed structure-function analyses and offers opportunities for evaluating FGF12 as a candidate for drug development or regenerative medicine applications. Overall, the study of recombinant FGF12 proteins holds promise for advancing our understanding of its role in both health and disease, providing insights that could lead to novel treatment strategies.
