Analytical Data
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Gene name
FBRS
- Application
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Alternative Names
FBRS; FBS; FBS1Probable fibrosin-1
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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
Q9HAH7
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Expression Region
1-460aa
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AA Sequence
MFEKYPGKMEGLFRHNPYTAFPPAVPGLPPGLPPAVSFGSLQGAFQPKSTNPELPPRLGPVPSGLSQKGTQIPDHFRPPLRKPGKWCAMHVRVAYMILRHQEKMKGDSHKLDFRNDLLPCLPGPYGALPPGQELSHPASLFTATGAVHAAANPFTAAPGAHGPFLSPSTHIDPFGRPTSFASLAALSNGAFGGLGSPTFNSGAVFAQKESPGAPPAFASPPDPWGRLHRSPLTFPAWVRPPEAARTPGSDKERPVERREPSITKEEKDRDLPFSRPQLRVSPATPKARAGEEGPRPTKESVRVKEERKEEAAAAAAAAAAAAAAAAAAATGPQGLHLLFERPRPPPFLGPSPPDRCAGFLEPTWLAAPPRLARPPRFYEAGEELTGPGAVAAARLYGLEPAHPLLYSRLAPPPPPAAAPGTPHLLSKTPPGALLGAPPPLVPAPRPSSPPRGPGPARADR
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Molecular Weight
48.3 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
FBRS (Fibrinogen-related protein B) is an important protein involved in various physiological and pathological processes, including inflammation, immune responses, and tissue repair. Its structure is characterized by a fibrinogen-like domain, which suggests a role in mediating protein-protein interactions and influencing biological pathways. Research into FBRS has gained traction due to its potential involvement in diseases such as cancer and cardiovascular disorders, where aberrant expression or function of fibrinogen-related proteins has been implicated. Understanding the biochemical properties and functional mechanisms of FBRS is crucial for elucidating its role in disease progression and for developing therapeutic strategies. Researchers have focused on recombinant protein techniques to produce FBRS in a controlled environment, allowing for detailed studies of its structure-function relationships. These recombinant proteins serve as valuable tools for investigating the biological activities of FBRS, enabling insights into how it interacts with other cellular components and contributes to various pathological states. Moreover, such studies may help identify FBRS as a potential biomarker or therapeutic target, paving the way for innovative approaches in treating related diseases. Thus, the exploration of FBRS and its recombinant forms is a promising avenue for advancing our understanding of its diverse biological roles and implications in health and disease.
