gs peptide Search Results


fluorescently-labeled glycogen synthase peptide substrate 5-fam-gs  (AnaSpec)
90
AnaSpec fluorescently-labeled glycogen synthase peptide substrate 5-fam-gs
Fluorescently Labeled Glycogen Synthase Peptide Substrate 5 Fam Gs, supplied by AnaSpec, 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/gs+peptide/10+aa+fluorescently+labeled+glycogen+synthase++5+fam+gs++peptide++5+fam+plsrtlsvss+nh2+/10__1002_slash_cmdc__201700503-144-15-20
Average 90 stars, based on 1 article reviews
fluorescently-labeled glycogen synthase peptide substrate 5-fam-gs - by Bioz Stars, 2026-09
90/100 stars
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gs-1 substrate  (Promega)
90
Promega gs-1 substrate
Gs 1 Substrate, supplied by Promega, 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/gs+peptide/gs+1+peptide+substrate/pmc07397174-702-22-24
Average 90 stars, based on 1 article reviews
gs-1 substrate - by Bioz Stars, 2026-09
90/100 stars
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gs peptide  (Bachem)
90
Bachem gs peptide
Gs Peptide, supplied by Bachem, 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/gs+peptide/gs+peptide/pm08224173-56-67-70
Average 90 stars, based on 1 article reviews
gs peptide - by Bioz Stars, 2026-09
90/100 stars
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gs-1 peptide (yrraavppspslsrhssphqspedeee)  (ProteinKinase)
90
ProteinKinase gs-1 peptide (yrraavppspslsrhssphqspedeee)
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Gs 1 Peptide (Yrraavppspslsrhssphqspedeee), supplied by ProteinKinase, 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/gs+peptide/gs+1+peptide++yrraavppspslsrhssphqspedeee/pmc06535550-412-6-12
Average 90 stars, based on 1 article reviews
gs-1 peptide (yrraavppspslsrhssphqspedeee) - by Bioz Stars, 2026-09
90/100 stars
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fluorescently-labeled glycogen synthase peptide substrate (5-fam-gs  (AnaSpec)
90
AnaSpec fluorescently-labeled glycogen synthase peptide substrate (5-fam-gs
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Fluorescently Labeled Glycogen Synthase Peptide Substrate (5 Fam Gs, supplied by AnaSpec, 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/gs+peptide/fluorescently+labeled+glycogen+synthase+peptide+substrate++5+fam+gs/pmc05962959-268-15-20
Average 90 stars, based on 1 article reviews
fluorescently-labeled glycogen synthase peptide substrate (5-fam-gs - by Bioz Stars, 2026-09
90/100 stars
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gs(332–346) peptide, acetylated-ekkgyfedrrpsanc-cooh  (ANYGEN Co)
90
ANYGEN Co gs(332–346) peptide, acetylated-ekkgyfedrrpsanc-cooh
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Gs(332–346) Peptide, Acetylated Ekkgyfedrrpsanc Cooh, supplied by ANYGEN 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/gs+peptide/gs+332+346++peptide++acetylated+ekkgyfedrrpsanc+cooh/pmc06794283-170-2-9
Average 90 stars, based on 1 article reviews
gs(332–346) peptide, acetylated-ekkgyfedrrpsanc-cooh - by Bioz Stars, 2026-09
90/100 stars
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me4(gs)3me4 synthetic peptide with amidated or cy3-modified c terminus and acetylated n terminus  (GenScript corporation)
90
GenScript corporation me4(gs)3me4 synthetic peptide with amidated or cy3-modified c terminus and acetylated n terminus
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Me4(gs)3me4 Synthetic Peptide With Amidated Or Cy3 Modified C Terminus And Acetylated N Terminus, supplied by GenScript corporation, 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/gs+peptide/me4+gs+3me4+synthetic+peptide+with+amidated+or+cy3+modified+c+terminus+and+acetylated+n+terminus/pm39633052-643-12-23
Average 90 stars, based on 1 article reviews
me4(gs)3me4 synthetic peptide with amidated or cy3-modified c terminus and acetylated n terminus - by Bioz Stars, 2026-09
90/100 stars
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peptides gs-1, gs-2, gs-3  (Bankpeptide biological technology co LTD)
90
Bankpeptide biological technology co LTD peptides gs-1, gs-2, gs-3
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Peptides Gs 1, Gs 2, Gs 3, supplied by Bankpeptide biological technology co LTD, 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/gs+peptide/peptides+gs+1++gs+2++gs+3/pmc05787506-69-3-9
Average 90 stars, based on 1 article reviews
peptides gs-1, gs-2, gs-3 - by Bioz Stars, 2026-09
90/100 stars
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flag-gs-ha peptide dykddddkggggsypydvpdya-nh 2  (LifeTein Inc)
90
LifeTein Inc flag-gs-ha peptide dykddddkggggsypydvpdya-nh 2
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Flag Gs Ha Peptide Dykddddkggggsypydvpdya Nh 2, supplied by LifeTein 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/gs+peptide/flag+gs+ha+peptide+standards+dykddddkggggsypydvpdya+amide/pmc08062696-478-0-10
Average 90 stars, based on 1 article reviews
flag-gs-ha peptide dykddddkggggsypydvpdya-nh 2 - by Bioz Stars, 2026-09
90/100 stars
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gs peptide  (Auspep Pty)
90
Auspep Pty gs peptide
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Gs Peptide, supplied by Auspep Pty, 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/gs+peptide/gs+peptide/pm09324113-34-21-35
Average 90 stars, based on 1 article reviews
gs peptide - by Bioz Stars, 2026-09
90/100 stars
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gs-1 peptide (yrraavppspslsrhssphqpsedeee  (GenScript corporation)
90
GenScript corporation gs-1 peptide (yrraavppspslsrhssphqpsedeee
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Gs 1 Peptide (Yrraavppspslsrhssphqpsedeee, supplied by GenScript corporation, 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/gs+peptide/gs+1+peptide++yrraavppspslsrhssphqpsedeee/10__3390_slash_molecules190915237-173-17-23
Average 90 stars, based on 1 article reviews
gs-1 peptide (yrraavppspslsrhssphqpsedeee - by Bioz Stars, 2026-09
90/100 stars
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recombinant spider venom peptide gs-ω/κ-hxtx-hv1h  (Vestaron Corporation)
90
Vestaron Corporation recombinant spider venom peptide gs-ω/κ-hxtx-hv1h
Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the <t>GSK3s</t> binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.
Recombinant Spider Venom Peptide Gs ω/κ Hxtx Hv1h, supplied by Vestaron Corporation, 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/gs+peptide/recombinant+spider+venom+peptide+gs+%CF%89+%CE%BA+hxtx+hv1h/pm36161468-0-23-32
Average 90 stars, based on 1 article reviews
recombinant spider venom peptide gs-ω/κ-hxtx-hv1h - by Bioz Stars, 2026-09
90/100 stars
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Image Search Results


Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the GSK3s binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.

Journal: Antimicrobial Agents and Chemotherapy

Article Title: Indirubin Analogues Inhibit Trypanosoma brucei Glycogen Synthase Kinase 3 Short and T. brucei Growth

doi: 10.1128/AAC.02065-18

Figure Lengend Snippet: Proposed mode of indirubin analogue binding to the active site of TbGSK3s. (A) Inhibitors 6-BIO (yellow carbons) and 10 (orange carbons) are shown as ball-and-stick models inside the GSK3s binding pocket, which is represented as a molecular surface colored according to its electrostatic potential (red, negative; blue, positive). The protonated piperazine ring of inhibitor 10 forms a charge-assisted hydrogen bond with the side chain of D171 (salt bridge), thus offering additional stabilization to the kinase-inhibitor complex (inset B), while the indirubin core is anchored at the hinge region mainly through two hydrogen bonds with the backbone atoms of V104 (inset C). (D) Side chain conformation of the arginine residue defining the binding cavity outer boundary in GSK3, as derived by MM-GBSA (molecular mechanisms, the generalized Born model and solvent accessibility) flexible docking calculations of 5-Me-6-BIO in the T. brucei (cyan, residue R110) and L. major (plum, residue R109) homologs. The difference in the flexibility of arginine originates from its intramolecular interaction with either E106 in T. brucei or the shorter side chain of D105 in L. major (not shown), possibly explaining the preference of indirubins for the trypanosomal homolog, where induced-fit effects can be accommodated more readily.

Article Snippet: For determining the kinase activity of Tb GSK3s, GS-1 peptide (YRRAAVPPSPSLSRHSSPHQSpEDEEE) ( proteinkinase.de ) was used as a substrate.

Techniques: Binding Assay, Residue, Derivative Assay, Solvent