TMEM41B Antibody recognizes endogenous levels of total TMEM41B protein.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human TMEM41B protein. Antibodies are purified by protein A and peptide affinity chromatography.

TMEM41B (also known as Stasimon) was discovered as a target of splicing dysfunction induced by loss of spinal motor neuron (SMN) protein, a feature of spinal muscular atrophy (SMA), resulting in motor circuit defects (1). Loss of TMEM41B in mice results in embryonic lethality (2). TMEM41B is a transmembrane protein that resides at the endoplasmic reticulum (ER) and is found at contact sites between the ER and mitochondria (2). Independent CRISPR screens identified TMEM41B as a novel regulator of autophagy, being structurally and functionally related to VMP1 (3-5). Loss of TMEM41B inhibited autophagosome formation and autophagic flux (3-5). Furthermore, depletion of TMEM41B led to an accumulation of lipid droplets, indicating a role in lipid mobilization and utilization of fatty acids (3,4). TMEM41B also appeared in screens, identifying it as an essential host protein for infection of flaviviruses and coronaviruses, including SARS-CoV-2 (6,7).