Analytical Data
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Gene name
VASH1
- Application
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Alternative Names
KIAA1036 (VASH)
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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
Q7L8A9
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Expression Region
1-204aa
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Molecular Weight
27.3 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
VASH1, or vasohibin-1, is a protein that plays a critical role in regulating angiogenesis, the process through which new blood vessels form from existing ones. It was first identified in studies related to vascular development and has since been recognized for its potential implications in various pathological conditions, including cancer, where abnormal blood vessel growth supports tumor progression. The research around VASH1 has gained momentum due to its dual functions: it acts as an anti-angiogenic factor while also being involved in endothelial cell function and migration. Investigating VASH1 recombinant proteins is important for understanding its mechanism of action and uncovering its therapeutic potential. Scientists aim to produce recombinant VASH1 to study its structure-function relationships, interactions with cellular pathways, and effects on endothelial cells in vitro and in vivo. This research could lead to novel therapeutic strategies for diseases characterized by abnormal angiogenesis, such as tumors and ocular diseases. Moreover, understanding the molecular underpinnings of VASH1 could provide insights into the broader regulatory networks involved in vascular biology, making this protein a significant target for future drug development and clinical applications in angiogenesis-related disorders.
