Analytical Data
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Gene name
FGF4
- Application
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Alternative Names
FGF4；HST；HSTF1；KS3；Fibroblast growth factor 4
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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
P08620
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Expression Region
31-206aa
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AA Sequence
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL
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Molecular Weight
22 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
Fibroblast Growth Factor 4 (FGF4) is a member of the FGF family, which plays a crucial role in various biological processes, including cell proliferation, differentiation, and tissue repair. Research on FGF4 has gained significant attention due to its involvement in developmental biology and its potential therapeutic applications. In embryonic development, FGF4 is known to influence limb formation and organogenesis, while in adults, it may contribute to wound healing and tissue regeneration. The recombinant protein form of FGF4 has been produced for research and clinical applications, allowing scientists to study its specific functions and interactions at the molecular level. Moreover, FGF4 has shown promise in regenerative medicine, particularly in enhancing stem cell proliferation and differentiation. Studies have also indicated its potential role in treating conditions like ischemic diseases and certain cancers, where promoting cell survival and growth can be beneficial. As researchers continue to explore the underlying mechanisms of FGF4, its therapeutic potential could expand, leading to novel treatments that harness its regenerative capabilities for various medical applications. The investigation of FGF4 recombinant protein, therefore, represents a vital area of study in both basic and applied biology, with the potential to contribute to advances in regenerative medicine and cancer therapy.
