Analytical Data
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Gene name
CST1
- Application
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Alternative Names
Cystatin SN; Salivary cystatin-SA-1
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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
P01037
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Expression Region
Trp21~Lys114
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Molecular Weight
16kDa
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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
CST1 (Cystatin S, also known as Cystatin SN) is a member of the cystatin family of cysteine proteinase inhibitors, playing a crucial role in the regulation of proteolytic enzymes involved in various biological processes. The research on CST1 has gained significant attention due to its potential implications in health and disease, particularly in relation to inflammation, cancer, and neurodegenerative disorders. Abnormal expression levels of CST1 have been linked to various pathological conditions, making it a promising biomarker for diagnostic and therapeutic purposes. Moreover, CST1's ability to inhibit cysteine proteases, such as cathepsins, which are implicated in the degradation of extracellular matrix components and modulation of immune responses, further highlights its importance in maintaining tissue homeostasis and regulating immune functions. Recent studies have focused on developing recombinant CST1 protein to investigate its structural properties and functional roles in disease mechanisms. This research involves various biochemical and molecular techniques, aiming to elucidate the role of CST1 in modulating protease activity and its potential therapeutic applications, including the design of CST1-based inhibitors. Understanding the comprehensive biological functions and clinical relevance of CST1 through recombinant protein studies may pave the way for innovative strategies to address diseases associated with cysteine protease dysregulation.
