Analytical Data
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Gene name
FGFB
- Application
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Alternative Names
FGFB；FGFB；Fibroblast growth factor 2
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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
P09038
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Expression Region
143-288aa
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AA Sequence
PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
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Molecular Weight
20.4 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
FGFB, or Fibroblast Growth Factor-2 (FGF-2), is a key member of the Fibroblast Growth Factor family, which plays crucial roles in various biological processes, including cell proliferation, differentiation, angiogenesis, and tissue repair. Research on FGFB has gained significance due to its potential therapeutic applications in regenerative medicine and oncology. Abnormal expression of FGFB has been linked to several diseases, including cancer, where it contributes to tumor growth and metastasis by promoting vascularization and enhancing cellular survival. The recombinant form of FGFB, generated through recombinant DNA technology, allows for detailed studies of its biological functions and interactions at a molecular level. This has facilitated the elucidation of its signaling pathways and the development of FGFB-based drugs. Moreover, the reconstitution of FGFB in laboratory settings helps in understanding its mechanisms of action, which can lead to novel treatment strategies for conditions characterized by impaired cell proliferation or tissue regeneration. As research progresses, FGFB continues to be a focal point for scientists aiming to unlock its full potential in therapeutic applications, paving the way for innovative solutions to complex medical challenges.
