GOT1 Protein, Human (His)

GOT1 Protein, Human (His), a recombinant human GOT1 produced in E. coli, has a His tag. Calcitonin has an effect on decreasing osteoclast activity and has the potential for hypercalcemia research. Reduction in glutamate concentration in blood is induced through the activity of the blood-resident enzyme glutamate oxaloacetate transaminase 1 (GOT1), which catalyzes the reversible transformation of oxaloacetate and glutamate to aspartate and α-ketoglutarate^[1].

Blood glutamate scavenging is a novel and attractive protecting strategy to reduce the excitotoxic effect of extracellular glutamate released during ischemic brain injury. Glutamate oxaloacetate transaminase 1 (GOT1) activation by means of oxaloacetate administration has been used to reduce the glutamate concentration in the blood^[1].

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

E. coli

C-6*His

P17174 (A2-Q413)

2805  [NCBI]

APPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQHHHHHH

Approximately 45.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.2 μm filter solution of 20 mM Tris-HCl, 100 mM NaCl, 2 mM DTT, 20% Glycerol, pH 7.5.

<1 EU/μg, determined by LAL method.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. M Pérez-Mato, et al. Human recombinant glutamate oxaloacetate transaminase 1 (GOT1) supplemented with oxaloacetate induces a protective effect after cerebral ischemia. Cell Death Dis. 2014 Jan 9;5(1):e992.  [Content Brief]