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Recombinant human integrin αvβ3

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Recombinant human integrin αVβ3 is a protein complex consisting of the alpha V and beta 3 integrin subunits. Integrins are cell surface receptors that mediate attachment between a cell and the extracellular matrix, or to other cells.

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Lab products found in correlation

Vitronectin, by R&D Systems (4 mentions) Cm7 chip, by GE Healthcare (4 mentions) Fibronectin, by Roche (4 mentions) Acetate buffer ph5, by GE Healthcare (3 mentions) Acetate buffer, by GE Healthcare (1 mentions) 125i echistatin, by PerkinElmer (1 mentions)

5 protocols using recombinant human integrin αvβ3

1

Integrin αVβ3 Binding Assay

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Example 13

Recombinant human integrin αVβ3 (R&D Systems, Minneapolis Minn.) was diluted to 40 ug/mL in Acetate buffer pH5.0 (GE Healthcare, Piscataway N.J.), and. then immobilized on a CM7 chip (GE Healthcare) using standard amine coupling techniques. 500 nM fibronectin (Roche Diagnostics, Indianapolis, Ind.) and vitronectin (R&D Systems) and 5 μM of either non-binding control 10Fn3 molecule (consisting of SEQ ID NO: 6 with an additional MG at the N-terminus and with a single amino acid substitution that changes RGD to RGE) or targeted 10Fn3 molecules (having a mutated FG loop that does not contain an RGD motif) were flowed over the top of the immobilized integrin. Binding RU was collected at the end of the sample injection. The results indicate that the lack of RGD in the FG loop results in abolishing binding of 10Fn3 molecules to fibronectin and vitronectin.

US10604556B2. Fibronectin binding domains with reduced immunogenicity (2020-03-31). BRISTOL-MYERS SQUIBB COMPANY [US]. Inventors: Jonathan Davis [US], Dasa Lipovsek [US], Ray Camphausen [US].
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2

Integrin αVβ3 Binding Inhibition

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Example 13

Recombinant human integrin αVβ3 (R&D Systems, Minneapolis Minn.) was diluted to 40 ug/mL in Acetate buffer pH5.0 (GE Healthcare, Piscataway N.J.), and. then immobilized on a CM7 chip (GE Healthcare) using standard amine coupling techniques. 500 nM fibronectin (Roche Diagnostics, Indianapolis, Ind.) and vitronectin (R&D Systems) and 5 μM of either non-binding control 10Fn3 molecule (consisting of SEQ ID NO: 6 with an additional MG at the N-terminus and with a single amino acid substitution that changes RGD to RGE) or targeted 10Fn3 molecules (having a mutated FG loop that does not contain an RGD motif) were flowed over the top of the immobilized integrin. Binding RU was collected at the end of the sample injection. The results indicate that the lack of RGD in the FG loop results in abolishing binding of 10Fn3 molecules to fibronectin and vitronectin.

US10464995B2. Fibronectin binding domains with reduced immunogenicity (2019-11-05). BRISTOL-MYERS SQUIBB COMPANY [US]. Inventors: Jonathan Davis [US], Dasa Lipovsek [US], Ray Camphausen [US].
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3

Integrin αVβ3 Binding Characterization

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Example 13

Recombinant human integrin αVβ3 (R&D Systems, Minneapolis Minn.) was diluted to 40 ug/mL in Acetate buffer pH5.0 (GE Healthcare, Piscataway N.J.), and. then immobilized on a CM7 chip (GE Healthcare) using standard amine coupling techniques. 500 nM fibronectin (Roche Diagnostics, Indianapolis, Ind.) and vitronectin (R&D Systems) and 5 μM of either non-binding control 10Fn3 molecule (consisting of SEQ ID NO: 6 with an additional MG at the N-terminus and with a single amino acid substitution that changes RGD to RGE) or targeted 10Fn3 molecules (having a mutated FG loop that does not contain an RGD motif) were flowed over the top of the immobilized integrin. Binding RU was collected at the end of the sample injection. The results indicate that the lack of RGD in the FG loop results in abolishing binding of 10Fn3 molecules to fibronectin and vitronectin.

US11447538B2. Fibronectin based scaffold proteins (2022-09-20). BRISTOL-MYERS SQUIBB COMPANY [US]. Inventors: Dasa Lipovsek [US], Jonathan H. Davis [US].
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4

Binding of 10Fn3 Molecules to Integrin

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Example 13

Recombinant human integrin αVβ3 (R&D Systems, Minneapolis Minn.) was diluted to 40 ug/mL in Acetate buffer pH 5.0 (GE Healthcare, Piscataway N.J.), and. then immobilized on a CM7 chip (GE Healthcare) using standard amine coupling techniques. 500 nM fibronectin (Roche Diagnostics, Indianapolis, Ind.) and vitronectin (R&D Systems) and 5 μM of either non-binding control 10Fn3 molecule (consisting of SEQ ID NO: 6 with an additional MG at the N-terminus and with a single amino acid substitution that changes RGD to RGE) or targeted 10Fn3 molecules (having a mutated FG loop that does not contain an RGD motif) were flowed over the top of the immobilized integrin. Binding RU was collected at the end of the sample injection. The results indicate that the lack of RGD in the FG loop results in abolishing binding of 10Fn3 molecules to fibronectin and vitronectin.

US11279751B2. Fibronectin binding domains with reduced immunogenicity (2022-03-22). Bristol-Myers Squibb Company [US]. Inventors: Jonathan Davis [US], Dasa Lipovsek [US], Ray Camphausen [US].
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5

Integrin αvβ3 Binding Assay

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Materials Unless otherwise noted, reagents and solvents were used as received from commercial sources. RGD tripeptide and echistatin were purchased from Wako (Japan) and Sigma (U.S.A.), respectively. [ 125 I]-Echistatin was from Perki-nElmer, Inc. (U.S.A.), and recombinant human integrin α v β 3 was from R&D Systems, Inc. (U.S.A.).
Makino A., Ueda M., Uematsu Y., Ohora T., Ohtani T., Miyagawa S., Fujibayashi Y., Okazawa H., Tokunaga Y, & Kiyono Y. (2022). Development of Low Molecular Weight Ligands for Integrin αvβ3. Chemical & pharmaceutical bulletin, 70(4).
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