Analytical Data
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Gene name
ITPA
- Application
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Alternative Names
ITPA;C20orf37;Inosine triphosphate pyrophosphatase
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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
Q9BY32
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Expression Region
3-180aa
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AA Sequence
ASLVGKKI VFVTGNAKKL EEVVQILGDK FPCTLVAQKI DLPEYQGEPD EISIQKCQEA VRQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLEKLKPEGL HQLLAGFEDK SAYALCTFAL STGDPSQPVR LFRGRTSGRI VAPRGCQDFG WDPCFQPDGY EQTYAEMPKA EKNAVSHRFR
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Molecular Weight
21 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
The study of ITPA (Inosine Triphosphate Pyrophosphatase) and its role in protein folding and restructuring has gained significant attention in recent years due to its implications in various biological processes and diseases. ITPA is an essential enzyme that catalyzes the hydrolysis of inosine triphosphate (ITP) to inosine monophosphate (IMP) and inorganic pyrophosphate. This enzymatic activity is crucial in maintaining nucleotide pools and preventing the accumulation of ITP, which can be detrimental to cellular function. Dysregulation of ITPA has been linked to several pathological conditions, including inflammatory diseases and certain types of cancer. Moreover, ITPA's involvement in the cellular stress response underscores its importance in protein homeostasis and the prevention of misfolding or aggregation of proteins. Researchers are increasingly focusing on the mechanistic insights of ITPA in cellular metabolism and its potential as a therapeutic target. Understanding the structure-function relationship of ITPA can provide valuable information for developing novel strategies to manage diseases associated with nucleotide metabolism. Consequently, exploring the restructured forms of ITPA may reveal how it can be modulated in various physiological and pathological contexts, making it a vital area for further investigation.
