Analytical Data
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Gene name
CST5
- Application
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Alternative Names
CST5;Cystatin-D
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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
P28325
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Expression Region
21-142aa
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AA Sequence
GSASAQSRTLAGGIHATDLNDKSVQCALDFAISEYNKVINKDEYYSRPLQ VMAAYQQIVG GVNYYFNVKFGRTTCTKSQPNLDNCPFNDQPKLKEEEF CSFQINEVPWEDKISILNYKCR KV
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Molecular Weight
15 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
CST5 (Cystatin M/E) is a member of the cystatin superfamily that plays a crucial role in regulating protease activity in various biological processes, including immune response, tissue remodeling, and cancer progression. Disruption of CST5 function has been implicated in several pathological conditions, making it a target of interest in biomedical research. The protein exhibits inhibitory effects on cathepsins, which are cysteine proteases involved in protein degradation and cellular signaling pathways. Recent studies have highlighted its potential as a biomarker for certain cancers and as a therapeutic target for modulating tumor microenvironments. The recombinant production of CST5 has enabled detailed studies of its structure-function relationships, leading to insights into its mechanistic roles in disease. Additionally, CST5's unique ability to influence cell behavior and promote apoptosis in malignant cells suggests its promise in developing new cancer therapies. As researchers continue to explore CST5's diverse functions and interactions, the understanding of its role in health and disease expands, paving the way for innovative approaches to targeting this protein in clinical settings. The ongoing investigation into CST5 and its recombinant form aims to unravel the complexities of cystatin family proteins and their potential applications in medicine.
