Analytical Data
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Gene name
TXNL4B
- Application
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Alternative Names
Dim1-like protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NX01
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Expression Region
1-149aa
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Molecular Weight
44 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
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Protein Description
VMO1, or Vascular Smooth Muscle Cell-Associated Protein 1, is a pivotal protein that has garnered significant attention in recent years due to its potential roles in vascular biology and disease. Initially identified as a protein expressed in vascular smooth muscle cells, VMO1 has been implicated in various physiological and pathological processes, including smooth muscle differentiation, proliferation, and apoptosis. Research indicates that VMO1 may play a crucial role in the development and progression of cardiovascular diseases, such as atherosclerosis and hypertension, by influencing vascular tone and remodeling. The understanding of VMO1's molecular mechanisms is further bolstered by its association with the regulation of several signaling pathways linked to cell growth and survival. Recent studies have aimed at elucidating the structure-function relationship of VMO1, as well as its interactions with other proteins, to provide insights into its biological significance. Moreover, the use of recombinant VMO1 protein in experimental studies presents an opportunity to explore therapeutic interventions that modulate its activity, potentially paving the way for novel approaches to treating vascular disorders. As the research community continues to unravel the complexities surrounding VMO1, this protein stands at the forefront of investigations aimed at understanding vascular health and developing effective cardiovascular therapies.
