sequence fragments of the heavy chain and light chain Search Results


90
Eurofins dna fragment encoding a heavy chain signal sequence and a human heavy chain g1 constant region
Dna Fragment Encoding A Heavy Chain Signal Sequence And A Human Heavy Chain G1 Constant Region, supplied by Eurofins, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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GenScript corporation l9 heavy and light chain sequences
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
L9 Heavy And Light Chain Sequences, 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
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90
LakePharma heavy- and light-chain variable region sequences
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Heavy And Light Chain Variable Region Sequences, supplied by LakePharma, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Microsynth ag sequencing of heavy and light chain variable regions
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Sequencing Of Heavy And Light Chain Variable Regions, supplied by Microsynth ag, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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BioAtla Inc double stranded dna fragments coding for the light chain and heavy chain cdr sequences
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Double Stranded Dna Fragments Coding For The Light Chain And Heavy Chain Cdr Sequences, supplied by BioAtla Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Entelechon GmbH genes encoding humanized v-region heavy (vh) and light (kappa, vk) chain sequences
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Genes Encoding Humanized V Region Heavy (Vh) And Light (Kappa, Vk) Chain Sequences, supplied by Entelechon GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Biointron Biological Inc antibodies light chain and heavy chain sequences
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Antibodies Light Chain And Heavy Chain Sequences, supplied by Biointron Biological Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Microsynth ag antibody heavy and light chains sequencing
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Antibody Heavy And Light Chains Sequencing, supplied by Microsynth ag, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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GenScript corporation heavy and light chains sequencing
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Heavy And Light Chains Sequencing, 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
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heavy and light chains sequencing - by Bioz Stars, 2026-05
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GenScript corporation chikv fab cap101a.e8 variable heavy and light chain cdnas bearing human il-2 signal sequences
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Chikv Fab Cap101a.E8 Variable Heavy And Light Chain Cdnas Bearing Human Il 2 Signal Sequences, 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
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Adaptive Biotechnologies Corp immunoglobulin heavy and light chain (vdj, dj, igk) high-throughput sequencing
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Immunoglobulin Heavy And Light Chain (Vdj, Dj, Igk) High Throughput Sequencing, supplied by Adaptive Biotechnologies Corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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AbbVie Inc sequences of the variable regions of the heavy and light chains
a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the <t>L9</t> <t>heavy</t> chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Sequences Of The Variable Regions Of The Heavy And Light Chains, supplied by AbbVie Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the L9 heavy chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9

doi: 10.1038/s41467-023-38509-2

Figure Lengend Snippet: a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the L9 heavy chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.

Article Snippet: L9 heavy and light chain sequences were synthesized and codon-optimized for mammalian expression and cloned into pHCMV3 by Genscript Inc.

Techniques: Binding Assay, Sequencing, Cryo-EM Sample Prep

a Ribbon diagram of Fab B (cyan) and C (maroon); side chains of interacting residues are shown. b – d Structural details of key homotypic interactions. Dashed lines indicate specific contacts. e Buried surface area (BSA) contributions of individual residues to the homotypic interface in L9 light chain. Sequence alignment with F10 K and germline IGKV1-5 gene is shown below. f Same as in e , for L9 heavy chain, with sequence alignment to F10 H and germline IGHV3-33 gene. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9

doi: 10.1038/s41467-023-38509-2

Figure Lengend Snippet: a Ribbon diagram of Fab B (cyan) and C (maroon); side chains of interacting residues are shown. b – d Structural details of key homotypic interactions. Dashed lines indicate specific contacts. e Buried surface area (BSA) contributions of individual residues to the homotypic interface in L9 light chain. Sequence alignment with F10 K and germline IGKV1-5 gene is shown below. f Same as in e , for L9 heavy chain, with sequence alignment to F10 H and germline IGHV3-33 gene. Source data are provided as a Source Data file.

Article Snippet: L9 heavy and light chain sequences were synthesized and codon-optimized for mammalian expression and cloned into pHCMV3 by Genscript Inc.

Techniques: Sequencing