Catalogue number
PRO-1131
Synonyms
NmrA-like family domain containing protein 1, short chain dehydrogenase/reductase family 48A member 1, HSCARG, SDR48A1, FLJ25918.
Introduction
NMRAL1 is a redox sensor protein which goes through reformation and subcellular rearrangement in reaction to alterations in intracellular NADPH/NADP+ levels. When the NADPH concentration is low the protein is found mostly as a monomer, and binds argininosuccinate synthase (ASS1), which takes part in nitric oxide synthesis. Association with ASS1 defects NMRAL1 activity and diminishes the production of nitric oxide, which then inhibits apoptosis. When the NADPH concentration is normal , the protein is found as a dimer and hides the for ASS1.
Description
NMRAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 323 amino acids (1-299) and having a molecular mass of 35.9 kDa.
NMRAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
The NMRAL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 40% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 95% as determined by SDS-PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSHMVDKKL VVVFGGTGAQ GGSVARTLLE DGTFKVRVVT RNPRKKAAKE LRLQGAEVVQ GDQDDQVIME LALNGAYATF IVTNYWESCS QEQEVKQGKL LADLARRLGL HYVVYSGLEN IKKLTAGRLA AAHFDGKGEV EEYFRDIGVP MTSVRLPCYF ENLLSHFLPQ KAPDGKSYLL SLPTGDVPMD GMSVSDLGPV VLSLLKMPEK YVGQNIGLST CRHTAEEYAA LLTKHTRKVV HDAKMTPEDY EKLGFPGARD LANMFRFYAL RPDRDIELTL RLNPKALTLD QWLEQHKGDF NLL
Safety Data Sheet
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
