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Aspartate Assay Kit - sufficient for 100colorimetricorfluorometrictests, high purity

  • sufficient for 100colorimetricorfluorometrictests
Item Number
A486313
Grouped product items
SKUSizeAvailabilityPrice Qty
A486313-1kit
1kit
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$1,121.90

Basic Description

Specifications & Puritysufficient for 100colorimetricorfluorometrictests
Storage TempStore at -20°C
Shipped InIce chest + Ice pads
Product Description

Aspartate, the carboxylate anion of aspartic acid, is an acidic, non-essential amino acid involved in protein synthesis and multiple other cellular biochemical pathways. Aspartate contributes to nucleotide synthesis via the synthesis of the precursor inosine mono-phosphate. In the urea cycle, aspartate is a key metabolite, donating a nitrogen group towards the formation of urea. Aspartate is also critical for oxidative phosphorylation as part of the aspartate-malate shuttle, which transfers reducing equivalents across the mitochondrial membrane.Aspartate Assay Kit has been used to measure the aspartate levels in nerve cells andLactococcus lactisstrain cultured in lysogeny broth (LB) medium.Suitability: The Aspartate Assay Kit is suitable for aspartate detection in cell and tissue culture supernatants, urine, plasma, serum, and other biological samples.Principle: Aspartate concentration is determined by a coupled enzyme assay, which results in a colorimetric (570 nm)/ fluorometric (λex = 535/λem = 587 nm) product, proportional to the aspartate present. Typical detection ranges for this kit are 2-10 nmole (colorimetric) and 0.2-1 nmole (fluorometric).

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References

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2. Xing Huang,Guangming Gan,Xiaoxiao Wang,Ting Xu,Wei Xie.  (2019-02-23)  The HGF-MET axis coordinates liver cancer metabolism and autophagy for chemotherapeutic resistance..  Autophagy,  15  ((7)): (1258-1279).  [PMID:30786811]
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4. Philip H Choi,Thu Minh Ngoc Vu,Huong Thi Pham,Joshua J Woodward,Mark S Turner,Liang Tong.  (2017-08-16)  Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria..  Proceedings of the National Academy of Sciences of the United States of America,  114  ((35)): (E7226-E7235).  [PMID:28808024]

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