Our mouse Malin FL594 conjugate monoclonal antibody from NeuroMab is produced in-house from clone N85/18. It detects human, mouse, non-human primate, and rat Malin and is purified by Protein A chromatography. Works in ICC.
NHL Repeat Containing E3 Ubiquitin Protein Ligase 1 is encoded by the gene NHLRC1. NHLRC1 is an E3 ubiquitin-protein ligase which is involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. NHLRC1 is expressed in the brain, spinal cord, heart, liver, skeletal muscle, and pancreas. Diseases associated with NHLRC1 include Myoclonic Epilepsy of Lafora and Epilepsy.
Purified by Protein A chromatography
Lot dependent: provided at 0.3-0.5 mg/mL
Monoclonal
N85/18
IgG1
ICC
Mouse
NHLRC1 EPM2B
42 kDa
Fusion protein amino acids 2-125 (N-terminus encompassing RING domain) of human Malin (also known as NHL repeat-containing protein 1, E3 ubiquitin-protein ligase NHLRC1, NHLRC1
and EPM2B, accession number Q6VVB1)
Human
Human, Mouse, Non-Human Primate, Rat
AB_2939478
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography and conjugation of purified mAb. Purified mAbs are >90% specific antibody.
PBS with 0.09% azide
FL594 Ex: 594 nm, Em: 615 nm
No cross-reactivity reported
Each new lot of antibody is quality control tested on cells overexpressing target protein and confirmed to give the expected staining pattern.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
12 months from date of receipt
EPM2A; E3 ubiquitin-protein ligase NHLRC1; MALIN; EC 2.3.2.27; bA204B7.2; NHL repeat-containing protein 1; NHL repeat containing 1; RING-type E3 ubiquitin transferase NHLRC1
Q6VVB1
UniProt Summary: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.
