Analytical Data
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Gene name
LTBP2
- Application
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Alternative Names
C14orf141; LTBP3
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14767
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Expression Region
Ser522~Thr814
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Molecular Weight
38kDa
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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
LTBP2 (Latent Transforming Growth Factor-beta Binding Protein 2) is a member of the LTBP family, which plays a crucial role in the regulation and activation of transforming growth factor-beta (TGF-β), a key cytokine involved in various biological processes, including tissue homeostasis, fibrosis, and immune response. The research into LTBP2 recombinant protein has gained momentum due to its potential implications in understanding pathological conditions such as fibrosis, cancer, and cardiovascular diseases, where TGF-β activity is often dysregulated. Investigating LTBP2 can provide insight into the extracellular matrix dynamics and TGF-β signaling pathways, shedding light on novel therapeutic targets for fibrotic diseases. Additionally, LTBP2's structural characteristics and its interactions with other extracellular matrix components contribute to the complexity of its functions, making it a subject of interest in developmental biology and regenerative medicine. The ability to produce LTBP2 as a recombinant protein offers a valuable tool for studying its biological functions in vitro and in vivo, facilitating studies that can unravel its role in health and disease. Understanding LTBP2's mechanisms may pave the way for innovative treatments and strategies to mitigate TGF-β-related pathologies, providing a clearer picture of the intricate balance between matrix remodeling and signaling in tissue repair and fibrosis.
