Analytical Data
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Gene name
CST4
- Application
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Alternative Names
CST4;Cystatin-S
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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
P01036
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Expression Region
21-141aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEA
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Molecular Weight
17 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
CST4, or cystatin F, is a member of the cystatin superfamily of proteins, which are known for their role as inhibitors of cysteine proteases. Recent studies have highlighted CST4's potential involvement in various biological processes, including immune responses, cell differentiation, and tissue remodeling. Investigations into CST4 have gained significance due to its implications in pathological conditions such as cancer and autoimmune diseases. Researchers have been focusing on recombinant protein technology to produce CST4 for further studies, as this allows for the generation of sufficient quantities of the protein with consistent quality for in vitro assays and functional analyses. The ability to study CST4 in detail may unveil its regulatory mechanisms and interactions within cellular pathways, contributing to a better understanding of its role in health and disease. Furthermore, recombinant CST4 could serve as a valuable tool for therapeutic applications, including targeted treatment strategies and the development of diagnostic markers. Overall, the study of CST4 recombinant protein is poised to provide insights into its multifaceted functions and therapeutic potential.
