Analytical Data
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Gene name
ITPRIPL1
- Application
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Alternative Names
ITPRIPL1; KIAA1754L; Inositol 1; 4; 5-trisphosphate receptor-interacting protein-like 1
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Species
Human
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6GPH6
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Expression Region
H25-G103
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Molecular Weight
40-43 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
ITPRIPL1, or Inositol 1,4,5-trisphosphate receptor interacting protein-like 1, has garnered attention in recent years due to its potential roles in calcium signaling and cell communication. Research indicates that ITPRIPL1 may interact with inositol trisphosphate receptors (IP3Rs), which are critical for mediating intracellular calcium release. This interaction suggests that ITPRIPL1 could play a pivotal role in modulating calcium homeostasis and various signaling pathways, influencing physiological processes ranging from muscle contraction to neurotransmitter release. Investigations into ITPRIPL1 have also linked it to various diseases, including neurologic disorders and certain cancers, where aberrant calcium signaling is a contributing factor. Understanding the structure and function of ITPRIPL1, as well as its interactions with IP3Rs and other cellular components, is crucial for elucidating its biological significance and potential therapeutic implications. With advancements in molecular biology techniques, such as recombinant protein expression systems, researchers are now better equipped to study ITPRIPL1's properties, functionality, and the exact mechanisms by which it influences calcium signaling, thus paving the way for novel insights into its role in health and disease.
