Analytical Data
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Gene name
CST3
- Application
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Alternative Names
CST3;Cleavage stimulation factor subunit 1
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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
P01034
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Expression Region
1-146aa
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AA Sequence
MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA
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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
CST3, or Cystatin C, is a cysteine protease inhibitor that plays a crucial role in various physiological and pathological processes, including immune response, tissue remodeling, and neurodegenerative diseases. Studies have shown that CST3 is significantly involved in the regulation of proteolytic enzymes, influencing cellular functions and interacting with key pathways in inflammation and apoptosis. The reorganization of CST3 into recombinant proteins offers a promising approach to elucidate its functional roles and therapeutic potentials. Recent research has highlighted the importance of CST3 in the context of Alzheimer's disease, where its reduced levels are associated with increased amyloid-beta aggregation, contributing to the progression of neurodegeneration. Furthermore, CST3 has been studied for its potential implications in cancer biology, where it may modulate tumor progression and metastasis through its regulatory effects on the microenvironment. By producing recombinant CST3 proteins, researchers can better explore its structural properties, interactions with other proteins, and mechanisms of action. This understanding could lead to novel diagnostic and therapeutic strategies aimed at targeting CST3-related pathways, thereby enhancing the treatment of diseases such as neurodegeneration and cancer. Consequently, the investigation of CST3 recombinant proteins represents a vital area of study with significant implications for advancing our knowledge of disease mechanisms and developing innovative therapeutic interventions.
