Analytical Data
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Gene name
Vasorin
- Application
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Alternative Names
SLITL2; Slit-Like 2
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Species
Mouse
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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
Q9CZT5
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Expression Region
Asn299~Ala559
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Molecular Weight
36kDa
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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
Vasorin is a glycoprotein that plays a crucial role in various physiological processes, including vascular development and remodeling. Identified as a soluble antagonist of the bone morphogenetic protein (BMP) signaling pathway, vasorin is particularly significant in the context of cardiovascular health. Dysregulation of BMP signaling has been implicated in conditions such as pulmonary hypertension and vascular malformations. The recombinant production of vasorin protein has become a focal point in recent research due to its potential therapeutic applications. Scientists aim to explore its effects on endothelial function and smooth muscle cell behavior, with the hope that the recombinant protein could serve as a biomarker or therapeutic agent for vascular-related diseases. Moreover, understanding the structure and function of vasorin can provide insights into its role in modulating the extracellular matrix and cellular interactions, ultimately leading to innovations in treating heart and vascular disorders. As research progresses, the recombinant form of vasorin not only enhances our understanding of vascular biology but also opens avenues for novel treatment strategies targeting BMP signaling pathways.
