inosine triphosphatase (nucleoside triphosphate pyrophosphatase), ELISA Kit

Mouse Inosine triphosphate pyrophosphatase (ITPA) ELISA kit; C20orf37; HLC14-06-P; ITPase; dJ794I6.3; My049 protein; inosine triphosphatase; inosine triphosphatase-A; inosine triphosphate pyrophosphohydrolase; nucleoside triphosphate diphosphatase; putative oncoge; inosine triphosphatase (nucleoside triphosphate pyrophosphatase)

For Research Use Only. Not for use in diagnostic procedures.

Store all reagents at 2-8 degree C

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Small volumes of ITPA elisa kit vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS9333175 is a ready-to-use microwell, strip plate ELISA (enzyme-linked immunosorbent assay) Kit for analyzing the presence of the inosine triphosphatase (nucleoside triphosphate pyrophosphatase) (ITPA) ELISA Kit target analytes in biological samples. The concentration gradients of the kit standards or positive controls render a theoretical kit detection range in biological research samples containing ITPA. The ELISA analytical biochemical technique of the MBS9333175 kit is based on ITPA antibody-ITPA antigen interactions (immunosorbency) and an HRP colorimetric detection system to detect ITPA antigen targets in samples. The ELISA Kit is designed to detect native, not recombinant, ITPA. Appropriate sample types may include undiluted body fluids and/or tissue homogenates, secretions. Quality control assays assessing reproducibility identified the intra-assay CV (%) and inter-assay CV(%).

21,897 Da

inosine triphosphatase (nucleoside triphosphate pyrophosphatase)

inosine triphosphate pyrophosphatase; ITPase; NTPase; nucleoside-triphosphate diphosphatase; non-standard purine NTP pyrophosphatase; nucleoside triphosphate pyrophosphatase; nucleoside-triphosphate pyrophosphatase; non-canonical purine NTP pyrophosphatase

Inosine triphosphate pyrophosphatase

ITPase; Inosine triphosphatase; NTPase  [Similar Products]

ITPA_MOUSE

ITPA: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Defects in ITPA are the cause of inosine triphosphate pyrophosphohydrolase deficiency (ITPAD). It is a common inherited trait characterized by the abnormal accumulation of inosine triphosphate (ITP) in erythrocytes and also leukocytes and fibroblasts. The pathological consequences of ITPA deficiency, if any, are unknown. However, it might have pharmacogenomic implications and be related to increased drug toxicity of purine analog drugs. Three different human populations have been reported with respect to their ITPase activity: high, mean (25% of high) and low activity. The variant Thr-32 is associated with complete loss of enzyme activity, may be by altering the local secondary structure of the protein. Heterozygotes for this polymorphism have 22.5% of the control activity: this is consistent with a dimeric structure of the enzyme. Belongs to the HAM1 NTPase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Nucleotide Metabolism - pyrimidine; Hydrolase; EC 3.6.1.19; Xenobiotic Metabolism - drug metabolism - other enzymes; Nucleotide Metabolism - purine

Cellular Component: cytoplasm

Molecular Function: hydrolase activity; metal ion binding; nucleotide binding; nucleoside-triphosphate diphosphatase activity

Biological Process: nucleoside triphosphate catabolic process; ITP catabolic process; nucleotide metabolic process; chromosome organization and biogenesis

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