Review





Similar Products

β4 pnks2 nachr subunits  (New England Biolabs)
99
New England Biolabs β4 pnks2 nachr subunits
β4 Pnks2 Nachr Subunits, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/%CE%B24+nachr+subunit/XbaI/pm30009767-65-7-18
Average 99 stars, based on 1 article reviews
β4 pnks2 nachr subunits - by Bioz Stars, 2026-09
99/100 stars
  Buy from Supplier
nachrs with α3, α5, β2, and β4 subunits  (Macklin Inc)
90
Macklin Inc nachrs with α3, α5, β2, and β4 subunits
Nachrs With α3, α5, β2, And β4 Subunits, supplied by Macklin Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/%CE%B24+nachr+subunit/nachrs+with+%CE%B13++%CE%B15++%CE%B22++and+%CE%B24+subunits/pmc11866872-173-2-22
Average 90 stars, based on 1 article reviews
nachrs with α3, α5, β2, and β4 subunits - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier
human α3, α4, β2 β4 nachr subunit cdnas plasmid pcdna3.1  (Merck & Co)
90
Merck & Co human α3, α4, β2 β4 nachr subunit cdnas plasmid pcdna3.1
Human α3, α4, β2 β4 Nachr Subunit Cdnas Plasmid Pcdna3.1, supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/%CE%B24+nachr+subunit/pcdna3/pmc03558472-135-11-16
Average 90 stars, based on 1 article reviews
human α3, α4, β2 β4 nachr subunit cdnas plasmid pcdna3.1 - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier
β4 nachr subunits  (New England Biolabs)
99
New England Biolabs β4 nachr subunits
Molecular docking of wild-type α-conotoxins Vc1.1, BuIA, ImI, and AuIB and their disulfide-deleted analogues (orange)at homology models of human nAChRs (the principal (+) subunit in green; the complementary (−) subunit in cyan). (A,B) Vc1.1 and Vc1.1[C2H,C8F] bound to the α10(+)α9(−) binding site of hα9α10 <t>nAChR.</t> (D,E) BuIA and BuIA[C2H,C8F] bound to the α3(+)β2(−) binding site of hα3β2 nAChR. (G,H) ImI and ImI[C2H,C8F] bound to the α10(+)α9(−) binding site of hα7 nAChR. (J,K) AuIB and AuIB[C2H,C8F] bound to the <t>α3(+)β4(−)</t> binding site of hα3β4 nAChR. The dashed lines show the H bond formed between pairwise interacting residues of the conotoxins and nAChRs. (C,F,I,L) Opening probability distribution for the C-loop of the human nAChRs for the wild-type α-conotoxin (blue) and the mutants (orange). The arrow indicates right shift movement of the nAChR C-loop.
β4 Nachr Subunits, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/%CE%B24+nachr+subunit/XbaI/pmc06044955-130-25-34
Average 99 stars, based on 1 article reviews
β4 nachr subunits - by Bioz Stars, 2026-09
99/100 stars
  Buy from Supplier
β4 nachr subunits  (Addgene inc)
90
Addgene inc β4 nachr subunits
Molecular docking of wild-type α-conotoxins Vc1.1, BuIA, ImI, and AuIB and their disulfide-deleted analogues (orange)at homology models of human nAChRs (the principal (+) subunit in green; the complementary (−) subunit in cyan). (A,B) Vc1.1 and Vc1.1[C2H,C8F] bound to the α10(+)α9(−) binding site of hα9α10 <t>nAChR.</t> (D,E) BuIA and BuIA[C2H,C8F] bound to the α3(+)β2(−) binding site of hα3β2 nAChR. (G,H) ImI and ImI[C2H,C8F] bound to the α10(+)α9(−) binding site of hα7 nAChR. (J,K) AuIB and AuIB[C2H,C8F] bound to the <t>α3(+)β4(−)</t> binding site of hα3β4 nAChR. The dashed lines show the H bond formed between pairwise interacting residues of the conotoxins and nAChRs. (C,F,I,L) Opening probability distribution for the C-loop of the human nAChRs for the wild-type α-conotoxin (blue) and the mutants (orange). The arrow indicates right shift movement of the nAChR C-loop.
β4 Nachr Subunits, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/%CE%B24+nachr+subunit/beta4-nAChR+(DPM+negative+control)+(Plasmid+%2386651)/10__1074_slash_jbc__m116__730804-308-10-21
Average 90 stars, based on 1 article reviews
β4 nachr subunits - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier

Image Search Results


Molecular docking of wild-type α-conotoxins Vc1.1, BuIA, ImI, and AuIB and their disulfide-deleted analogues (orange)at homology models of human nAChRs (the principal (+) subunit in green; the complementary (−) subunit in cyan). (A,B) Vc1.1 and Vc1.1[C2H,C8F] bound to the α10(+)α9(−) binding site of hα9α10 nAChR. (D,E) BuIA and BuIA[C2H,C8F] bound to the α3(+)β2(−) binding site of hα3β2 nAChR. (G,H) ImI and ImI[C2H,C8F] bound to the α10(+)α9(−) binding site of hα7 nAChR. (J,K) AuIB and AuIB[C2H,C8F] bound to the α3(+)β4(−) binding site of hα3β4 nAChR. The dashed lines show the H bond formed between pairwise interacting residues of the conotoxins and nAChRs. (C,F,I,L) Opening probability distribution for the C-loop of the human nAChRs for the wild-type α-conotoxin (blue) and the mutants (orange). The arrow indicates right shift movement of the nAChR C-loop.

Journal: ACS Omega

Article Title: Role of Cys I –Cys III Disulfide Bond on the Structure and Activity of α-Conotoxins at Human Neuronal Nicotinic Acetylcholine Receptors

doi: 10.1021/acsomega.7b00639

Figure Lengend Snippet: Molecular docking of wild-type α-conotoxins Vc1.1, BuIA, ImI, and AuIB and their disulfide-deleted analogues (orange)at homology models of human nAChRs (the principal (+) subunit in green; the complementary (−) subunit in cyan). (A,B) Vc1.1 and Vc1.1[C2H,C8F] bound to the α10(+)α9(−) binding site of hα9α10 nAChR. (D,E) BuIA and BuIA[C2H,C8F] bound to the α3(+)β2(−) binding site of hα3β2 nAChR. (G,H) ImI and ImI[C2H,C8F] bound to the α10(+)α9(−) binding site of hα7 nAChR. (J,K) AuIB and AuIB[C2H,C8F] bound to the α3(+)β4(−) binding site of hα3β4 nAChR. The dashed lines show the H bond formed between pairwise interacting residues of the conotoxins and nAChRs. (C,F,I,L) Opening probability distribution for the C-loop of the human nAChRs for the wild-type α-conotoxin (blue) and the mutants (orange). The arrow indicates right shift movement of the nAChR C-loop.

Article Snippet: Plasmid pMXT construct of the human α7 nAChR subunit was linearized with BamHI , and plasmid pT7TS constructs of human α3, α9, α10, β2, and β4 nAChR subunits were linearized with XbaI restriction enzymes (NEB, Ipswich, MA) for in vitro cRNA transcription using SP6 (hα7) and T7 (hα3, α9, α10, β2, and β4) mMessage mMachine transcription kits (AMBION, Foster City, CA).

Techniques: Binding Assay