GDA Mouse
Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.
Greater than 95.0% as determined by SDS-PAGE.
Description
GDA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 477 amino acids (1-454 a.a) and having a molecular mass of 53.4kDa.
GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.
MGSSHHHHHH SSGLVPRGSH MGSMCAARTP PLALVFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE SSQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHAPQ YAFAGSNVDL PLLEWLNKYT FPTEQRFRST DVAEEVYTRV VRRTLKNGTT TACYFGTIHT DSSLILAEIT DKFGQRAFVG KVCMDLNDTV PEYKETTEES VKETERFVSE MLQKNYPRVK PIVTPRFTLS CTETLMSELG NIAKTHDLYI QSHISENREE IEAVKSLYPS YKNYTDVYDK NNLLTNKTVM AHGCYLSEEE LNIFSERGAS IAHCPNSNLS LSSGLLNVLE VLKHKVKIGL GTDVAGGYSY SMLDAIRRAV MVSNVLLINK VNEKNLTLKE VFRLATLGGS QALGLDSEIG NFEVGKEFDA LLINPRASDS PIDLFYGDFV GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.
Product Science Overview
The recombinant form of mouse guanine deaminase is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein often includes a His-tag at the N-terminus to facilitate purification . The full-length mouse guanine deaminase consists of 454 amino acids and has a molecular weight of approximately 53.4 kDa .
Guanine deaminase is responsible for converting guanine to xanthine, which is subsequently converted to uric acid by the enzyme xanthine oxidase. This process is vital for maintaining the balance of purine nucleotides within the cell. The enzyme’s activity is defined as the amount of enzyme that converts guanine to xanthine per minute at a specific pH and temperature .
In addition to its role in purine metabolism, guanine deaminase has been identified as a cytosolic regulator of PSD-95 postsynaptic targeting . PSD-95 is a protein involved in the organization of synaptic signaling complexes, which are crucial for synaptic plasticity and neuronal communication. This regulatory function highlights the enzyme’s importance beyond its metabolic role.
Recombinant mouse guanine deaminase is widely used in research to study its enzymatic activity, structure-function relationships, and its role in various biological processes. The recombinant protein is often utilized in enzyme activity assays, structural studies, and as a control in various experimental setups .
The recombinant mouse guanine deaminase is typically stored at -20°C to maintain its stability and activity. It is important to avoid repeated freeze-thaw cycles to prevent degradation of the protein . The protein is usually supplied in a buffer containing Tris-HCl, NaCl, DTT, and glycerol to ensure its stability during storage and handling .
