Review



short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2  (GenScript corporation)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90

    Structured Review

    GenScript corporation short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2
    Short Peptide Dimers [Akpsypptyk] 2 And [Akp*Syp*P*Tyk] 2, 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/result/short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2 - by Bioz Stars, 2026-02
    90/100 stars

    Images



    Similar Products

    90
    Mimetics short peptide mimetics of the b7-1 dimer interface
    Short Peptide Mimetics Of The B7 1 Dimer Interface, supplied by Mimetics, 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/result/short peptide mimetics of the b7-1 dimer interface/product/Mimetics
    Average 90 stars, based on 1 article reviews
    short peptide mimetics of the b7-1 dimer interface - by Bioz Stars, 2026-02
    90/100 stars
      Buy from Supplier

    90
    Mimetics short peptide mimetics of the b7-2 dimer interface
    Conservation of the β-strand(8)/hinge/α-helix(4) domain in the bacterial superantigen family. (A) Amino acid sequences of the β-strand(8)/hinge/α-helix(4) domain (residues 145-156 in SEA) in representative streptococcal <t>superantigens</t> (top) and staphylococcal superantigens (bottom). Names of superantigens studied here are highlighted in blue. (B,C) The β-strand(8)/hinge/α-helix(4) domain shows high structural conservation among diverse superantigens . In cartoon structure of SEA [5fk9.pdb; ], the β-strand(8)/hinge/α-helix(4) domain is depicted in red, residues contacting the TCR are in blue, and residues contacting the MHC-II in orange (B) . Degree of amino acid sequence conservation among superantigens is mapped onto the SEA structure using Consurf (C) .
    Short Peptide Mimetics Of The B7 2 Dimer Interface, supplied by Mimetics, 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/result/short peptide mimetics of the b7-2 dimer interface/product/Mimetics
    Average 90 stars, based on 1 article reviews
    short peptide mimetics of the b7-2 dimer interface - by Bioz Stars, 2026-02
    90/100 stars
      Buy from Supplier

    90
    GenScript corporation short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2
    Conservation of the β-strand(8)/hinge/α-helix(4) domain in the bacterial superantigen family. (A) Amino acid sequences of the β-strand(8)/hinge/α-helix(4) domain (residues 145-156 in SEA) in representative streptococcal <t>superantigens</t> (top) and staphylococcal superantigens (bottom). Names of superantigens studied here are highlighted in blue. (B,C) The β-strand(8)/hinge/α-helix(4) domain shows high structural conservation among diverse superantigens . In cartoon structure of SEA [5fk9.pdb; ], the β-strand(8)/hinge/α-helix(4) domain is depicted in red, residues contacting the TCR are in blue, and residues contacting the MHC-II in orange (B) . Degree of amino acid sequence conservation among superantigens is mapped onto the SEA structure using Consurf (C) .
    Short Peptide Dimers [Akpsypptyk] 2 And [Akp*Syp*P*Tyk] 2, 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/result/short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    short peptide dimers [akpsypptyk] 2 and [akp*syp*p*tyk] 2 - by Bioz Stars, 2026-02
    90/100 stars
      Buy from Supplier

    90
    GenScript corporation short peptide dimers
    Conservation of the β-strand(8)/hinge/α-helix(4) domain in the bacterial superantigen family. (A) Amino acid sequences of the β-strand(8)/hinge/α-helix(4) domain (residues 145-156 in SEA) in representative streptococcal <t>superantigens</t> (top) and staphylococcal superantigens (bottom). Names of superantigens studied here are highlighted in blue. (B,C) The β-strand(8)/hinge/α-helix(4) domain shows high structural conservation among diverse superantigens . In cartoon structure of SEA [5fk9.pdb; ], the β-strand(8)/hinge/α-helix(4) domain is depicted in red, residues contacting the TCR are in blue, and residues contacting the MHC-II in orange (B) . Degree of amino acid sequence conservation among superantigens is mapped onto the SEA structure using Consurf (C) .
    Short Peptide Dimers, 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/result/short peptide dimers/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    short peptide dimers - by Bioz Stars, 2026-02
    90/100 stars
      Buy from Supplier

    90
    Mimetics short peptide mimetics of the cd28 dimer interface
    Conservation of the β-strand(8)/hinge/α-helix(4) domain in the bacterial superantigen family. (A) Amino acid sequences of the β-strand(8)/hinge/α-helix(4) domain (residues 145-156 in SEA) in representative streptococcal <t>superantigens</t> (top) and staphylococcal superantigens (bottom). Names of superantigens studied here are highlighted in blue. (B,C) The β-strand(8)/hinge/α-helix(4) domain shows high structural conservation among diverse superantigens . In cartoon structure of SEA [5fk9.pdb; ], the β-strand(8)/hinge/α-helix(4) domain is depicted in red, residues contacting the TCR are in blue, and residues contacting the MHC-II in orange (B) . Degree of amino acid sequence conservation among superantigens is mapped onto the SEA structure using Consurf (C) .
    Short Peptide Mimetics Of The Cd28 Dimer Interface, supplied by Mimetics, 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/result/short peptide mimetics of the cd28 dimer interface/product/Mimetics
    Average 90 stars, based on 1 article reviews
    short peptide mimetics of the cd28 dimer interface - by Bioz Stars, 2026-02
    90/100 stars
      Buy from Supplier

    Image Search Results


    Conservation of the β-strand(8)/hinge/α-helix(4) domain in the bacterial superantigen family. (A) Amino acid sequences of the β-strand(8)/hinge/α-helix(4) domain (residues 145-156 in SEA) in representative streptococcal superantigens (top) and staphylococcal superantigens (bottom). Names of superantigens studied here are highlighted in blue. (B,C) The β-strand(8)/hinge/α-helix(4) domain shows high structural conservation among diverse superantigens . In cartoon structure of SEA [5fk9.pdb; ], the β-strand(8)/hinge/α-helix(4) domain is depicted in red, residues contacting the TCR are in blue, and residues contacting the MHC-II in orange (B) . Degree of amino acid sequence conservation among superantigens is mapped onto the SEA structure using Consurf (C) .

    Journal: Frontiers in Immunology

    Article Title: Staphylococcal and Streptococcal Superantigens Trigger B7/CD28 Costimulatory Receptor Engagement to Hyperinduce Inflammatory Cytokines

    doi: 10.3389/fimmu.2019.00942

    Figure Lengend Snippet: Conservation of the β-strand(8)/hinge/α-helix(4) domain in the bacterial superantigen family. (A) Amino acid sequences of the β-strand(8)/hinge/α-helix(4) domain (residues 145-156 in SEA) in representative streptococcal superantigens (top) and staphylococcal superantigens (bottom). Names of superantigens studied here are highlighted in blue. (B,C) The β-strand(8)/hinge/α-helix(4) domain shows high structural conservation among diverse superantigens . In cartoon structure of SEA [5fk9.pdb; ], the β-strand(8)/hinge/α-helix(4) domain is depicted in red, residues contacting the TCR are in blue, and residues contacting the MHC-II in orange (B) . Degree of amino acid sequence conservation among superantigens is mapped onto the SEA structure using Consurf (C) .

    Article Snippet: Short peptide mimetics of the B7-2 dimer interface bind diverse superantigens, prevent binding of SEB to cell-surface B7-2 or CD28, inhibit superantigen-mediated induction of interleukin-2, IFN-γ and tumor necrosis factor in human PBMC, and are effective in vivo , protecting mice from lethal SEB challenge ( , ).

    Techniques: Sequencing

    Staphylococcal and streptococcal superantigens trigger intercellular CD28/B7-2 synapse formation. (A–E) HEK293T cells transfected in triplicate to express CD28/GFP fusion protein (green label) were incubated with HEK293T cells transfected to express B7-2/Cherry fusion protein (red label), in absence (blue bars) or presence of the indicated superantigen at concentrations shown (red orange bars). As negative control served B7-2C/Cherry, which lacks the ability to bind CD28 (cyan bars). Intercellular CD28/B7-2-dependent synapse formation was scored using flow cytometry to quantitate per cent doubly labeled cells (error bars, SEM; n = 3). Comparisons were made using one-tailed unpaired Student's t -test; * p < 0.05, ** p < 0.005, **** p < 0.0001.

    Journal: Frontiers in Immunology

    Article Title: Staphylococcal and Streptococcal Superantigens Trigger B7/CD28 Costimulatory Receptor Engagement to Hyperinduce Inflammatory Cytokines

    doi: 10.3389/fimmu.2019.00942

    Figure Lengend Snippet: Staphylococcal and streptococcal superantigens trigger intercellular CD28/B7-2 synapse formation. (A–E) HEK293T cells transfected in triplicate to express CD28/GFP fusion protein (green label) were incubated with HEK293T cells transfected to express B7-2/Cherry fusion protein (red label), in absence (blue bars) or presence of the indicated superantigen at concentrations shown (red orange bars). As negative control served B7-2C/Cherry, which lacks the ability to bind CD28 (cyan bars). Intercellular CD28/B7-2-dependent synapse formation was scored using flow cytometry to quantitate per cent doubly labeled cells (error bars, SEM; n = 3). Comparisons were made using one-tailed unpaired Student's t -test; * p < 0.05, ** p < 0.005, **** p < 0.0001.

    Article Snippet: Short peptide mimetics of the B7-2 dimer interface bind diverse superantigens, prevent binding of SEB to cell-surface B7-2 or CD28, inhibit superantigen-mediated induction of interleukin-2, IFN-γ and tumor necrosis factor in human PBMC, and are effective in vivo , protecting mice from lethal SEB challenge ( , ).

    Techniques: Transfection, Incubation, Negative Control, Flow Cytometry, Labeling, One-tailed Test

    Staphylococcal and streptococcal superantigens trigger CD28/B7-1 synapse formation. (A–C) HEK293T cells transfected in triplicate to express CD28/GFP fusion protein (green label) were incubated with HEK293T cells transfected to express B7-1/Cherry fusion protein (red label), in absence (blue bars) or presence of the indicated superantigen at concentrations shown (red orange bars). As negative control served B7-2C/Cherry, which lacks the ability to bind CD28 (cyan bars). Intercellular CD28/B7-1-dependent synapse formation was scored using flow cytometry to quantitate per cent doubly labeled cells (error bars, SEM; n = 3). Comparisons were made using one-tailed unpaired Student's t -test; ** p < 0.005, *** p < 0.001, **** p < 0.0001.

    Journal: Frontiers in Immunology

    Article Title: Staphylococcal and Streptococcal Superantigens Trigger B7/CD28 Costimulatory Receptor Engagement to Hyperinduce Inflammatory Cytokines

    doi: 10.3389/fimmu.2019.00942

    Figure Lengend Snippet: Staphylococcal and streptococcal superantigens trigger CD28/B7-1 synapse formation. (A–C) HEK293T cells transfected in triplicate to express CD28/GFP fusion protein (green label) were incubated with HEK293T cells transfected to express B7-1/Cherry fusion protein (red label), in absence (blue bars) or presence of the indicated superantigen at concentrations shown (red orange bars). As negative control served B7-2C/Cherry, which lacks the ability to bind CD28 (cyan bars). Intercellular CD28/B7-1-dependent synapse formation was scored using flow cytometry to quantitate per cent doubly labeled cells (error bars, SEM; n = 3). Comparisons were made using one-tailed unpaired Student's t -test; ** p < 0.005, *** p < 0.001, **** p < 0.0001.

    Article Snippet: Short peptide mimetics of the B7-2 dimer interface bind diverse superantigens, prevent binding of SEB to cell-surface B7-2 or CD28, inhibit superantigen-mediated induction of interleukin-2, IFN-γ and tumor necrosis factor in human PBMC, and are effective in vivo , protecting mice from lethal SEB challenge ( , ).

    Techniques: Transfection, Incubation, Negative Control, Flow Cytometry, Labeling, One-tailed Test