Analytical Data
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Gene name
tsr
- Application
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Alternative Names
tsr；Pre-rRNA-processing Protein TSR2 homolog
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Species
E.coli
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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
P02942
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Expression Region
211-551aa
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AA Sequence
WFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF
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Molecular Weight
38.0 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
TSR (Thrombospondin Type 1 Domain) recombinant proteins have garnered significant interest in biomedical research due to their crucial roles in cellular processes such as cell adhesion, migration, and angiogenesis. Originally identified as a component of the extracellular matrix, TSR domains are known for their ability to interact with various cellular receptors and extracellular matrix proteins, thereby influencing cell behavior and signaling pathways. In recent years, researchers have focused on the therapeutic potential of TSR domain-containing proteins in various diseases, including cancer, where they may act as tumor suppressors, and cardiovascular disorders, where they may contribute to the regulation of blood vessel formation. The ability to produce TSR recombinant proteins in sufficient quantities allows for detailed studies on their biochemical properties and interactions, enabling the exploration of their functional applications in drug development and tissue engineering. Furthermore, investigations into the structural characteristics of TSR domains using techniques such as X-ray crystallography and NMR have provided insights into their mechanisms of action, paving the way for the design of targeted therapies that harness their biological activities. As the understanding of TSR proteins continues to evolve, their utilization in clinical settings holds promise for innovative treatments aimed at modulating complex biological processes.
