research use only
Cat.No.: F5124
| Dilution |
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|
| Application |
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| WB, IHC, IF |
| Reactivity |
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| Human, Mouse, Rat, Pig |
| Source |
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| Mouse Monoclonal Antibody |
| Storage Buffer |
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| PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 |
| Storage (from the date of receipt) |
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| -20°C (avoid freeze-thaw cycles), 2 years |
| Predicted MW Observed MW |
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| 30 kDa 30 kDa |
| *Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. |
| Specificity |
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| TMEM111 Antibody [B9P11] detects endogenous levels of total TMEM111 protein. |
| Clone |
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| B9P11 |
| Synonym(s) |
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| ER membrane protein complex subunit 3; Transmembrane protein 111; EMC3; TMEM111 |
| Background |
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| TMEM111, or Transmembrane Protein 111, is an integral endoplasmic reticulum membrane protein of about 26 kilodaltons and is part of the TMEM family of poorly characterized multi-spanning membrane proteins that help regulate protein quality control and cellular homeostasis in tissues such as the brain, liver, and kidney. TMEM111 is a small, hydrophobic protein with multiple predicted transmembrane domains that form an intramembrane scaffold, and it has cytoplasmic loops that interact with ER-associated degradation machinery and the Bag3 chaperone complex, though its specific motifs and residues are not well-defined due to limited structural data. Its main function is to coordinate the ubiquitin-proteasome and ER-associated degradation pathways by tethering misfolded proteins to degradation complexes, facilitating their ubiquitination through E2 conjugases, and preventing toxic protein aggregation during ER stress, thus maintaining proteostasis and cell viability. TMEM111 also supports the Bag3-HSP70-HSC70 chaperone network to selectively degrade aggregation-prone proteins, connects ER stress responses to autophagy, and ensures proper protein turnover through lysosomal and proteasomal routes. When TMEM111 is dysfunctional, ER-associated degradation becomes less efficient, leading to protein accumulation implicated in diseases such as Alzheimer's, due to amyloid processing defects, and liver disorders from impaired hepatocyte homeostasis. |
| References |
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