resource source identifier antibodies rabbit polyclonal anti tmem106b (Proteintech)
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resource source identifier antibodies rabbit polyclonal anti tmem106b
Resource Source Identifier Antibodies Rabbit Polyclonal Anti Tmem106b, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/resource source identifier antibodies rabbit polyclonal anti tmem106b/product/Proteintech
Average 93 stars, based on 21 article reviews
Resource Source Identifier Antibodies Rabbit Polyclonal Anti Tmem106b, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/resource source identifier antibodies rabbit polyclonal anti tmem106b/product/Proteintech
Average 93 stars, based on 21 article reviews
resource source identifier antibodies rabbit polyclonal anti tmem106b - by Bioz Stars,
2026-03
93/100 stars
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1) Product Images from "Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases."
Article Title: Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases.
Journal: Cell
doi: 10.1016/j.cell.2022.02.026
Figure Legend Snippet: Figure 1. Overview of native TMEM106B (A) Schematic view of TMEM106B with its N-ter- minal domain (NTD), transmembrane domain (TM), and C-terminal domain (CTD). (B) A predicted structure of TMEM106B from ROBETTA (Kim et al., 2004) colored with the same scheme as (A), indicating sites at which the C-terminal domain may get cleaved. (C) Aggregation propensity mapped onto a pre- dicted structure of TMEM106B(120–254) from AlphaFold (Jumper et al., 2021) (positive values in blue indicate soluble regions and negative values in red correspond to aggregation-prone regions).
Techniques Used:
Figure Legend Snippet: Figure 2. Cryo-EM reconstructions of TMEM106B fibrils Cross-sections (10 z-slice average) of the TMEM106B(120–254) singlet and doublet fibril unsharpened density maps from eight cases of FTLD-TDP, two cases of PSP, and one case of DLB. See also Figures S1–S3 and S6 and Tables S2 and S3.
Techniques Used: Cryo-EM Sample Prep
Figure Legend Snippet: Figure 3. Cryo-EM structure of a TMEM106B doublet fibril Cryo-EM density (mesh) and atomic model (sticks) of (A) a TMEM106B doublet fibril and (B) the interface between the two protofilaments in the TMEM106B doublet fibril mediated by a non-proteinaceous, anionic cofactor (purple mesh) that binds to the sidechains of residues K178 and R180 of each protofilament. See also Figure S5 and Table S2.
Techniques Used: Cryo-EM Sample Prep
Figure Legend Snippet: Figure 4. Cryo-EM structure of a TMEM106B protofilament highlighting the key structural features (A) Cryo-EM density (mesh) and atomic model (sticks) of a TMEM106B protofilament. (B) A disulfide bond between C214 and C253. (C) Polymorphic site T185S and glycosylated asparagine at N183. (D–F) Glycosylated N164 (D), N151 (E), and N145 (F). See also Figures S4 and S5 and Table S2.
Techniques Used: Cryo-EM Sample Prep
Figure Legend Snippet: Figure 5. Cryo-EM structure of a highly twisted TMEM106B singlet fibril and comparison of singlet fibril molecular polymorphs (A) Cryo-EM density (mesh) and atomic model (sticks) of a highly twisted TMEM106B singlet fibril. (B) Magnified view of an unknown density bound to K178 in a highly twisted TMEM106B singlet fibril. (C) Overlay of the atomic models (Ca chain shown) of the low-twist (green) and high-twist (pink) singlet fibrils. (D) Comparison of secondary structure motifs formed by the low-twist (green) singlet fibril, high-twist (pink) singlet fibril, and native protein predicted by AlphaFold (blue) with experimentally determined post-translational modifications of the highly twisted TMEM106B singlet fibril. See also Figure S5 and Table S2.
Techniques Used: Cryo-EM Sample Prep, Comparison
Figure Legend Snippet: Figure 6. Structure-based model of a possible interrelationship between TMEM106B, aggregated filaments, and lysosomes in neurodegenerative diseases Under physiological conditions, TMEM106B spans the lysosomal/endosomal membrane. Upon cleavage of the C-terminal fragment, TMEM106B(120–254) fibrils may form. It is currently unknown whether TMEM106B(120–254) fibrillizes in the lumen or whether lysosomal leakage occurs and TMEM106B(120–254) fragments aggregate into fibrils in the cytosol. Based on our set of TMEM106B fibril structures, we speculate that the aggregation of TMEM106B(120–254) into fibrils leads to lysosomal dysfunction, which promotes the accumulation of aberrantly aggregated amyloid fibrils such as those formed by TDP-43 (PDB:7PY2, green sticks), tau (PDB:7P65, blue sticks), or a-synuclein.
Techniques Used: Membrane