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k03.12 fab fragment crystallization  (Thermo Fisher)


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    Structured Review

    Thermo Fisher k03.12 fab fragment crystallization
    (A) Phylogram of <t>K03.12</t> clonal antibody lineage, K03.1-12. Lineage members characterized further are in red. Avin for rHA (H3 WI-05) of each member in parentheses. (B) Affinities of Fab fragments from selected lineage members for HA heads of seasonal H1 and H3 HAs that circulated during the donor’s lifetime. Coloring according to the key indicates the apparent equilibrium dissociation constant (KD), measured by biolayer interferometry using a “single hit” Fab concentration of 30μM. A second round of screening using UCA, K03.12 and K03.1 returned equivalent values. (C) Affinity maturation of lineage K03.1-12. KDs of lineage members for H1-FL-00 and H3 TX-12. See also Figure S5 and Table S2 and Supplemental Data Sets 1 and 2.
    K03.12 Fab Fragment Crystallization, supplied by Thermo Fisher, 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/k03%2E12+fab+fragment+crystallization/pmc05810956-538-1-11
    Average 90 stars, based on 1 article reviews
    k03.12 fab fragment crystallization - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires"

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires

    Journal: Immunity

    doi: 10.1016/j.immuni.2017.12.009

    (A) Phylogram of K03.12 clonal antibody lineage, K03.1-12. Lineage members characterized further are in red. Avin for rHA (H3 WI-05) of each member in parentheses. (B) Affinities of Fab fragments from selected lineage members for HA heads of seasonal H1 and H3 HAs that circulated during the donor’s lifetime. Coloring according to the key indicates the apparent equilibrium dissociation constant (KD), measured by biolayer interferometry using a “single hit” Fab concentration of 30μM. A second round of screening using UCA, K03.12 and K03.1 returned equivalent values. (C) Affinity maturation of lineage K03.1-12. KDs of lineage members for H1-FL-00 and H3 TX-12. See also Figure S5 and Table S2 and Supplemental Data Sets 1 and 2.
    Figure Legend Snippet: (A) Phylogram of K03.12 clonal antibody lineage, K03.1-12. Lineage members characterized further are in red. Avin for rHA (H3 WI-05) of each member in parentheses. (B) Affinities of Fab fragments from selected lineage members for HA heads of seasonal H1 and H3 HAs that circulated during the donor’s lifetime. Coloring according to the key indicates the apparent equilibrium dissociation constant (KD), measured by biolayer interferometry using a “single hit” Fab concentration of 30μM. A second round of screening using UCA, K03.12 and K03.1 returned equivalent values. (C) Affinity maturation of lineage K03.1-12. KDs of lineage members for H1-FL-00 and H3 TX-12. See also Figure S5 and Table S2 and Supplemental Data Sets 1 and 2.

    Techniques Used: Concentration Assay

    (A) Structure of K03.12 bound with HA head of H3 TX-12. (B) Contacts made by HCDR3 of K03.12 with conserved residues of the RBS; conserved HA residues, in cyan; K03.12 HCDR3, in purple. (C) Structure of UCA bound with HA head of H1 SI-06. The SI-06 HA head is in the same orientation as the TX-12 head in Fig. 4A. (D) Contacts made by the UCA HCDR3 with conserved residues of the RBS. Conserved HA residues are in light green; the UCA HCDR3, in orange. See also Figure S6.
    Figure Legend Snippet: (A) Structure of K03.12 bound with HA head of H3 TX-12. (B) Contacts made by HCDR3 of K03.12 with conserved residues of the RBS; conserved HA residues, in cyan; K03.12 HCDR3, in purple. (C) Structure of UCA bound with HA head of H1 SI-06. The SI-06 HA head is in the same orientation as the TX-12 head in Fig. 4A. (D) Contacts made by the UCA HCDR3 with conserved residues of the RBS. Conserved HA residues are in light green; the UCA HCDR3, in orange. See also Figure S6.

    Techniques Used:

    (A) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the UCA-SI-06 complex (light green). Red asterisk: bulge spanning residues 131-135 (including 133a) in H1 CA-09. (B) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the K03.12 - H3 TX-12 complex (purple and cyan, respectively). Red asterisk: close approach of K03.12 HCDR3 and bulge in H1 CA-09. (C) Comparison of H1 (SI-06) and H3 (TX-12) backbones between residues 131 and 135. Red asterisk: polypeptide chain backbones of H1 (SI-06) and H3 TX-12 at position 133. Stick-representation of side-chain: residue 152, Leu or Ile in H1 HAs; Asn in H3 HAs. Dotted line: interaction in H3 HAs of the polypeptide chain backbone at position 133 with the side chain of Asn152.
    Figure Legend Snippet: (A) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the UCA-SI-06 complex (light green). Red asterisk: bulge spanning residues 131-135 (including 133a) in H1 CA-09. (B) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the K03.12 - H3 TX-12 complex (purple and cyan, respectively). Red asterisk: close approach of K03.12 HCDR3 and bulge in H1 CA-09. (C) Comparison of H1 (SI-06) and H3 (TX-12) backbones between residues 131 and 135. Red asterisk: polypeptide chain backbones of H1 (SI-06) and H3 TX-12 at position 133. Stick-representation of side-chain: residue 152, Leu or Ile in H1 HAs; Asn in H3 HAs. Dotted line: interaction in H3 HAs of the polypeptide chain backbone at position 133 with the side chain of Asn152.

    Techniques Used:

    (A) HA-Fab complexes of UCA, K03.12 and C05 (PDB 4FP8) superposed on HA on H3 TX-12. The HCDR3 of each Fab K03.12 (purple), UCA (orange), C05 (green) is shown in stick representation. (B) Amino acid sequence alignment of HCDR3 in K03.12 lineage members and in antibody C05. Identical residues are in red. See also Figure S6.
    Figure Legend Snippet: (A) HA-Fab complexes of UCA, K03.12 and C05 (PDB 4FP8) superposed on HA on H3 TX-12. The HCDR3 of each Fab K03.12 (purple), UCA (orange), C05 (green) is shown in stick representation. (B) Amino acid sequence alignment of HCDR3 in K03.12 lineage members and in antibody C05. Identical residues are in red. See also Figure S6.

    Techniques Used: Sequencing

    Related Articles

    Crystallization Assay:

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires
    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Produced:

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires
    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Transfection:

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires
    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Concentration Assay:

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires
    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Sequencing:

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires
    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.



    Similar Products

    k03.12 fab fragment crystallization  (Thermo Fisher)
    90
    Thermo Fisher k03.12 fab fragment crystallization
    (A) Phylogram of <t>K03.12</t> clonal antibody lineage, K03.1-12. Lineage members characterized further are in red. Avin for rHA (H3 WI-05) of each member in parentheses. (B) Affinities of Fab fragments from selected lineage members for HA heads of seasonal H1 and H3 HAs that circulated during the donor’s lifetime. Coloring according to the key indicates the apparent equilibrium dissociation constant (KD), measured by biolayer interferometry using a “single hit” Fab concentration of 30μM. A second round of screening using UCA, K03.12 and K03.1 returned equivalent values. (C) Affinity maturation of lineage K03.1-12. KDs of lineage members for H1-FL-00 and H3 TX-12. See also Figure S5 and Table S2 and Supplemental Data Sets 1 and 2.
    K03.12 Fab Fragment Crystallization, supplied by Thermo Fisher, 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/k03%2E12+fab+fragment+crystallization/pmc05810956-538-1-11
    Average 90 stars, based on 1 article reviews
    k03.12 fab fragment crystallization - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) Phylogram of K03.12 clonal antibody lineage, K03.1-12. Lineage members characterized further are in red. Avin for rHA (H3 WI-05) of each member in parentheses. (B) Affinities of Fab fragments from selected lineage members for HA heads of seasonal H1 and H3 HAs that circulated during the donor’s lifetime. Coloring according to the key indicates the apparent equilibrium dissociation constant (KD), measured by biolayer interferometry using a “single hit” Fab concentration of 30μM. A second round of screening using UCA, K03.12 and K03.1 returned equivalent values. (C) Affinity maturation of lineage K03.1-12. KDs of lineage members for H1-FL-00 and H3 TX-12. See also Figure S5 and Table S2 and Supplemental Data Sets 1 and 2.

    Journal: Immunity

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires

    doi: 10.1016/j.immuni.2017.12.009

    Figure Lengend Snippet: (A) Phylogram of K03.12 clonal antibody lineage, K03.1-12. Lineage members characterized further are in red. Avin for rHA (H3 WI-05) of each member in parentheses. (B) Affinities of Fab fragments from selected lineage members for HA heads of seasonal H1 and H3 HAs that circulated during the donor’s lifetime. Coloring according to the key indicates the apparent equilibrium dissociation constant (KD), measured by biolayer interferometry using a “single hit” Fab concentration of 30μM. A second round of screening using UCA, K03.12 and K03.1 returned equivalent values. (C) Affinity maturation of lineage K03.1-12. KDs of lineage members for H1-FL-00 and H3 TX-12. See also Figure S5 and Table S2 and Supplemental Data Sets 1 and 2.

    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Techniques: Concentration Assay

    (A) Structure of K03.12 bound with HA head of H3 TX-12. (B) Contacts made by HCDR3 of K03.12 with conserved residues of the RBS; conserved HA residues, in cyan; K03.12 HCDR3, in purple. (C) Structure of UCA bound with HA head of H1 SI-06. The SI-06 HA head is in the same orientation as the TX-12 head in Fig. 4A. (D) Contacts made by the UCA HCDR3 with conserved residues of the RBS. Conserved HA residues are in light green; the UCA HCDR3, in orange. See also Figure S6.

    Journal: Immunity

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires

    doi: 10.1016/j.immuni.2017.12.009

    Figure Lengend Snippet: (A) Structure of K03.12 bound with HA head of H3 TX-12. (B) Contacts made by HCDR3 of K03.12 with conserved residues of the RBS; conserved HA residues, in cyan; K03.12 HCDR3, in purple. (C) Structure of UCA bound with HA head of H1 SI-06. The SI-06 HA head is in the same orientation as the TX-12 head in Fig. 4A. (D) Contacts made by the UCA HCDR3 with conserved residues of the RBS. Conserved HA residues are in light green; the UCA HCDR3, in orange. See also Figure S6.

    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Techniques:

    (A) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the UCA-SI-06 complex (light green). Red asterisk: bulge spanning residues 131-135 (including 133a) in H1 CA-09. (B) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the K03.12 - H3 TX-12 complex (purple and cyan, respectively). Red asterisk: close approach of K03.12 HCDR3 and bulge in H1 CA-09. (C) Comparison of H1 (SI-06) and H3 (TX-12) backbones between residues 131 and 135. Red asterisk: polypeptide chain backbones of H1 (SI-06) and H3 TX-12 at position 133. Stick-representation of side-chain: residue 152, Leu or Ile in H1 HAs; Asn in H3 HAs. Dotted line: interaction in H3 HAs of the polypeptide chain backbone at position 133 with the side chain of Asn152.

    Journal: Immunity

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires

    doi: 10.1016/j.immuni.2017.12.009

    Figure Lengend Snippet: (A) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the UCA-SI-06 complex (light green). Red asterisk: bulge spanning residues 131-135 (including 133a) in H1 CA-09. (B) Polypeptide backbone of H1 CA-09 (PDB 3UBE) (gray) superposed on HA backbone in the K03.12 - H3 TX-12 complex (purple and cyan, respectively). Red asterisk: close approach of K03.12 HCDR3 and bulge in H1 CA-09. (C) Comparison of H1 (SI-06) and H3 (TX-12) backbones between residues 131 and 135. Red asterisk: polypeptide chain backbones of H1 (SI-06) and H3 TX-12 at position 133. Stick-representation of side-chain: residue 152, Leu or Ile in H1 HAs; Asn in H3 HAs. Dotted line: interaction in H3 HAs of the polypeptide chain backbone at position 133 with the side chain of Asn152.

    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Techniques:

    (A) HA-Fab complexes of UCA, K03.12 and C05 (PDB 4FP8) superposed on HA on H3 TX-12. The HCDR3 of each Fab K03.12 (purple), UCA (orange), C05 (green) is shown in stick representation. (B) Amino acid sequence alignment of HCDR3 in K03.12 lineage members and in antibody C05. Identical residues are in red. See also Figure S6.

    Journal: Immunity

    Article Title: Memory B cells that cross-react with group 1 and group 2 influenza A viruses are abundant in adult human repertoires

    doi: 10.1016/j.immuni.2017.12.009

    Figure Lengend Snippet: (A) HA-Fab complexes of UCA, K03.12 and C05 (PDB 4FP8) superposed on HA on H3 TX-12. The HCDR3 of each Fab K03.12 (purple), UCA (orange), C05 (green) is shown in stick representation. (B) Amino acid sequence alignment of HCDR3 in K03.12 lineage members and in antibody C05. Identical residues are in red. See also Figure S6.

    Article Snippet: The K03.12 Fab fragment for crystallization was produced by Lipofectamine 2000 (Thermo Fisher) facilitated, transient transfection of 293T cells.

    Techniques: Sequencing