Analytical Data
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Gene name
FBLN5
- Application
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Alternative Names
FBLN5；DANCE；Fibulin-5
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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
Q9UBX5
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Expression Region
24-448aa
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AA Sequence
QAQCTNG FDLDRQSGQC LDIDECRTIP EACRGDMMCV NQNGGYLCIP RTNPVYRGPY SNPYSTPYSG PYPAAAPPLS APNYPTISRP LICRFGYQMD ESNQCVDVDE CATDSHQCNP TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL CANVPGSYSC TCNPGFTLNE DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE DGVHCSDMDE CSFSEFLCQH ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPREIQLDL EMITVNTVIN FRGSSVIRLR IYVSQYPF
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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
FBLN5, or Fibulin-5, is a member of the fibulin family of extracellular matrix proteins, which play crucial roles in tissue development, maintenance, and repair. The importance of FBLN5 has been highlighted in various studies linking it to cardiovascular health, particularly in elastogenesis, where it contributes to the assembly of elastic fibers in vascular tissues. Abnormalities in FBLN5 expression or function are implicated in several pathological conditions, including aortic aneurysms and disorders related to connective tissues. Additionally, research has shown that FBLN5 interaction with other matrix components, such as integrins and growth factors, modulates cellular behaviors, influencing processes like cell adhesion, migration, and proliferation. To further investigate its biological functions and potential therapeutic applications, researchers have taken to producing recombinant FBLN5 proteins. These recombinant forms enable detailed studies of its structure-function relationships, interactions with other proteins, and roles in cellular signaling pathways. Understanding FBLN5’s mechanisms can provide insights into its roles in health and disease and may lead to innovations in regenerative medicine and targeted therapies for cardiovascular and connective tissue disorders. Overall, the study of FBLN5 and its recombinant proteins is critical for elucidating the complex dynamics of the extracellular matrix and its implications in various diseases.
