Analytical Data
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Gene name
SPHAR
- Application
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Alternative Names
SPHAR; Protein SPHAR; S-phase response protein
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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
Q15513
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Expression Region
1-63aa
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AA Sequence
MTRIKISVCI CFRYFEFCFF YALNILFQKV SEANSQTELL LRPHCKNILF NVSFMIDLQA AHF
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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
The study of SPHAR recombinant proteins has gained significant interest in the field of biotechnology and biomedical research due to their potential applications in various therapeutic areas. SPHAR, which stands for Specific Protein with Heterogeneous Activity, is characterized by its ability to perform multiple functions in biological systems. Research has shown that SPHAR proteins can play crucial roles in disease mechanisms, cell signaling, and immune responses. The recombinant production of SPHAR allows for a controlled and scalable generation of these proteins, enabling researchers to investigate their structure-function relationships, stability, and interaction with other biomolecules. Moreover, by leveraging advanced techniques such as genetic engineering and protein expression systems, scientists aim to enhance the properties of SPHAR proteins for applications in drug development, vaccine design, and targeted therapies. Understanding the underlying mechanisms of SPHAR proteins through recombinant technology can lead to novel biopharmaceuticals, contributing to the advancement of precision medicine and improving therapeutic outcomes for various diseases. This research is further supported by the increasing demand for innovative biological products and the need for more effective treatment strategies in healthcare.
