TMEM41B Antibody - BSA Free Summary
| Description |
Novus Biologicals Rabbit TMEM41B Antibody - BSA Free (NBP2-83692) is a polyclonal antibody validated for use in WB. All Novus Biologicals antibodies are covered by our 100% guarantee. |
| Immunogen |
The immunogen is a synthetic peptide directed towards the middle region of mouse TMEM41B. Peptide sequence: VMFLVYKNFPQLSEEERVNMKVPRDMDDAKALGKVLSKYKDTFYVQVLVA The peptide sequence for this immunogen was taken from within the described region. |
| Clonality |
Polyclonal |
| Host |
Rabbit |
| Gene |
TMEM41B |
| Purity |
Affinity purified |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
| Buffer |
PBS, 2% Sucrose |
| Preservative |
0.09% Sodium Azide |
| Concentration |
0.5 mg/ml |
| Purity |
Affinity purified |
Alternate Names for TMEM41B Antibody - BSA Free
Background
Transmembrane protein 41B/Stasimon (human TMEM41B theoretical molecular weight 32.5 kDa) is an integral endoplasmic reticulum membrane protein that plays a role in autophagy and neurogenesis (1). TMEM41B forms a complex with vacuole membrane protein 1 (VMP1) and is required for autophagosome formation. Similar to VMP1, TMEM41B contains a VTT domain. Expression of TMEM41B/Stasimon restores motor neuron function defects in Drosophila and zebrafish models of spinal muscular atrophy (SMA). Survival motor neuron protein (SMN) deficiency, which underscores the neuromuscular disorder SMA, affects TMEM41B/Stasimon U12 splicing and mRNA expression (2,3).
1. Stavoe, A. K. H., & Holzbaur, E. L. F. (2019). Autophagy in Neurons. Annual Review of Cell and Developmental Biology. https://doi.org/10.1146/annurev-cellbio-100818-125242
2. Doktor, T. K., Hua, Y., Andersen, H. S., Br0ner, S., Liu, Y. H., Wieckowska, A., Andresen, B. S. (2017). RNA-sequencing of a mouse-model of spinal muscular atrophy reveals tissue-wide changes in splicing of U12-dependent introns. Nucleic Acids Research. https://doi.org/10.1093/nar/gkw731
3. Hosseinibarkooie, S., Schneider, S., & Wirth, B. (2017). Advances in understanding the role of disease-associated proteins in spinal muscular atrophy. Expert Review of Proteomics. https://doi.org/10.1080/14789450.2017.1345631
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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