Analytical Data
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Gene name
sip
- Application
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Species
Streptococcus agalactiae
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9EU98
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Expression Region
26-434aa
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Molecular Weight
50.5 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
SIP (Sphingosine-1-phosphate receptor interacting protein) is a protein that has garnered attention in recent years due to its significant role in various cellular processes, such as cell signaling, migration, and survival. Research into SIP's structure and function has been driven by its implication in several diseases, including cancer, cardiovascular disorders, and neurodegenerative conditions. In cancer biology, SIP has been found to influence tumor progression and metastasis, making it a potential target for therapeutic interventions. Additionally, its involvement in the modulation of immune responses suggests that SIP could play a crucial role in inflammatory diseases. Recent advances in proteomics and molecular biology techniques have enabled researchers to elucidate the intricate signaling pathways associated with SIP. Investigating the molecular mechanisms underlying SIP's action could provide insights into its functional diversity and establish it as a biomarker or therapeutic target. The ongoing exploration into SIP's structure and interactions within cells is, therefore, critical for developing novel strategies for disease intervention and improving our understanding of cellular dynamics in health and disease. As research continues, SIP's relevance in the intricate web of cellular communication underscores its potential significance in biomedicine.
