ASNS Mouse
Sf9, Insect cells.
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
Greater than 95.0% as determined by SDS-PAGE.
Description
ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.
ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Asparagine synthetase (ASNS) is an enzyme that catalyzes the formation of asparagine from aspartate. This enzyme is crucial for cell growth and proliferation, and its expression is often elevated in cancer cells. In mice, ASNS is primarily expressed in the liver and brain.
Mouse ASNS, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain comprising 568 amino acids (1-562 a.a.) with a molecular weight of 65.2 kDa. It includes a 6-amino acid His tag at the C-terminus and is purified using proprietary chromatographic methods.
The ASNS protein solution (0.25 mg/ml) is supplied in PBS (pH 7.4) containing 40% glycerol.
Purity is greater than 95.0% as assessed by SDS-PAGE analysis.
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
Sf9, Insect cells.
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK AHHHHHH.
Product Science Overview
ASNS is a cytoplasmic enzyme that is chiefly responsible for generating asparagine from aspartate . The enzyme’s structure has been extensively studied in Escherichia coli, where it is found to be a dimeric protein with each subunit folding into two distinct domains . The N-terminal region consists of two layers of six-stranded antiparallel β-sheets, which house the active site responsible for the hydrolysis of glutamine . The C-terminal domain, on the other hand, is responsible for binding both Mg²⁺ ATP and aspartate . These two active sites are connected by a tunnel that allows for the passage of an ammonia molecule, facilitating the coupling of the two half-reactions carried out in the independent active sites of the enzyme .
Elevated ASNS protein expression has been associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia . This resistance is due to the enzyme’s ability to synthesize asparagine, which is essential for the survival of leukemia cells . Additionally, mutations in the ASNS gene have been linked to a condition known as asparagine synthetase deficiency (ASD), which is characterized by developmental delays, intellectual disability, microcephaly, intractable seizures, and progressive brain atrophy .
Recombinant ASNS from mouse models is often used in research to study the enzyme’s function and its role in various diseases. The recombinant form is produced by cloning the ASNS gene from mice into an expression vector, which is then introduced into a host cell for protein production. This allows researchers to obtain large quantities of the enzyme for biochemical and structural studies.
Mouse recombinant ASNS is invaluable in understanding the enzyme’s mechanism and its implications in disease. By studying the recombinant enzyme, researchers can gain insights into how ASNS activity is regulated and how its dysregulation contributes to disease. This knowledge can potentially lead to the development of targeted therapies for conditions associated with ASNS abnormalities.
