Analytical Data
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Gene name
FSBP
- Application
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Alternative Names
FSBP;Fibrinogen silencer-binding 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
O95073
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Expression Region
1-299aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMVGKARSSNFTLSEKLDLLKLVKPYVK ILEEHTNKHSVIVEKNRCWDIIAVNYNAIGVDRPPRTAQGLRTLYKRLKE YAKQELLQQKETQSDFKSNISEPTKKVMEMIPQISSFCLVRDRNHIQSAN LDEEAQAGTSSLQVMLDHHPVAITVEVKQEEDIKPPPPLVLNSQQSDTLE QREEHELVHVMERSLSPSLSSVDMRMTSSPSSIPRRDDFFRHESGEHFRS LLGYDPQILQMLKEEHQIILENQKNFGLYVQEKRDGLKRRQQLEEELLRA KIEVEKLKAIRLRHDLPEYNSL
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Molecular Weight
37 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
FSBP (Fibroblast Growth Factor 2 Binding Protein) is a protein that plays a crucial role in a variety of cellular processes, including cell proliferation, differentiation, and angiogenesis. Its involvement in numerous physiological and pathological conditions, such as wound healing, cancer, and tissue regeneration, has spurred considerable interest in understanding its structure and function. Recent advances in recombinant DNA technology have enabled the production of FSBP in higher quantities and with increased purity, facilitating in-depth studies of its properties. Researchers aim to elucidate the molecular mechanisms underlying FSBP interactions with fibroblast growth factors (FGFs) and to explore its potential as a therapeutic target. Furthermore, characterizing the recombinant FSBP allows for the development of novel biomaterials and regenerative medicine applications. The ability to manipulate and study FSBP in laboratory settings has accelerated research efforts aimed at discovering new interventions for diseases involving impaired regeneration or abnormal FGF signaling. Understanding the functional dynamics of FSBP can ultimately lead to improved strategies for tissue engineering and the treatment of various diseases, marking it as a significant focus within the realm of biomedical research.
