Analytical Data
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Gene name
FBLN7
- Application
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Alternative Names
FBLN7；TM14；Fibulin-7
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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
Q53RD9
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Expression Region
25-439aa
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AA Sequence
QNCLSKQQLLSAIRQLQQLLKGQETRFAEGIRHMKSRLAALQNSVGRVGPDALPVSCPALNTPADGRKFGSKYLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCRGISECSSQPCQNGGTCVEGVNQYRCICPPGRTGNRCQHQAQTAAPEGSVAGDSAFSRAPRCAQVERAQHCSCEAGFHLSGAAGDSVCQDVNECELYGQEGRPRLCMHACVNTPGSYRCTCPGGYRTLADGKSCEDVDECVGLQPVCPQGTTCINTGGSFQCVSPECPEGSGNVSYVKTSPFQCERNPCPMDSRPCRHLPKTISFHYLSLPSNLKTPITLFRMATASAPGRAGPNSLRFGIVGGNSRGHFVMQRSDRQTGDLILVQNLEGPQTLEVDVDMSEYLDRSFQANHVSKVTIFVSPYDF
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Molecular Weight
51.7 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
FBLN7, or fibulin-7, is a member of the fibulin family of extracellular matrix (ECM) glycoproteins, which are known for their critical roles in tissue development, stability, and cellular adhesion. Research into FBLN7 has garnered interest due to its potential implications in various biological processes, including cell proliferation, differentiation, and migration. It is thought to be involved in the regulation of ECM structures, influencing cellular responses in physiological and pathological contexts. Elevated FBLN7 expression has been associated with certain cancers, suggesting a role in tumor progression and metastasis, while its function in normal tissue homeostasis highlights its importance in developmental biology. Understanding the molecular mechanisms and signaling pathways related to FBLN7 can provide insights into its potential as a therapeutic target in diseases characterized by fibrosis and impaired wound healing. Recombinant FBLN7 protein studies can facilitate the exploration of its interactions with other ECM components and cell surface receptors, thus enhancing our understanding of its role in health and disease. Additionally, elucidating the structure-function relationship of FBLN7 is essential for harnessing its potential in regenerative medicine and tissue engineering, where ECM components are crucial for promoting cell function and tissue regeneration. As research progresses, the characterization of FBLN7 and the implications of its recombinant form could pave the way for novel diagnostic and therapeutic strategies, particularly in cancer biology and regenerative therapies.
