anti human icam 1 mab  (Sino Biological)


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    ICAM 1 Matched ELISA Antibody Pair Set Human
    Description:
    Each vial contains 22 ng of recombinant Human ICAM 1 CD54 Reconstitute with 1 mL detection antibody dilution buffer After reconstitution store at 20℃ to 80℃ in a manual defrost freezer A seven point standard curve using 2 fold serial dilutions in sample dilution buffer and a high standard of 300 pg mL is recommended
    Catalog Number:
    SEKA10346
    Price:
    None
    Category:
    Elisa pair set
    Reactivity:
    Human
    Product Aliases:
    BB2 Matched ELISA Antibody Pair Set Human, CD54 Matched ELISA Antibody Pair Set Human, ICAM-1 Matched ELISA Antibody Pair Set Human, P3.58 Matched ELISA Antibody Pair Set Human
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    Structured Review

    Sino Biological anti human icam 1 mab
    A conserved tyrosine residue within the MD regions of α X , α M , and α D negatively regulates TH-induced integrin activation. ( A–C) TH-induced <t>ICAM-1</t> binding. The relatively conserved tyrosine was mutated to phenylalanine in all α L -chimeras ( A – C ), and to glutamic acid or alanine in the α L -α M chimera ( C ). A conserved methionine was also mutated to alanine in the α L -α M chimera ( C ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated α L constructs plus β 2 -D709A and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. Data are presented as the MFI of the ICAM-1 binding normalized to integrin expression and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras or their mutants to α L -WT under the GFP-TH condition, or as indicated (*P
    Each vial contains 22 ng of recombinant Human ICAM 1 CD54 Reconstitute with 1 mL detection antibody dilution buffer After reconstitution store at 20℃ to 80℃ in a manual defrost freezer A seven point standard curve using 2 fold serial dilutions in sample dilution buffer and a high standard of 300 pg mL is recommended
    https://www.bioz.com/result/anti human icam 1 mab/product/Sino Biological
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti human icam 1 mab - by Bioz Stars, 2021-04
    91/100 stars

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    1) Product Images from "The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation"

    Article Title: The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-23444-w

    A conserved tyrosine residue within the MD regions of α X , α M , and α D negatively regulates TH-induced integrin activation. ( A–C) TH-induced ICAM-1 binding. The relatively conserved tyrosine was mutated to phenylalanine in all α L -chimeras ( A – C ), and to glutamic acid or alanine in the α L -α M chimera ( C ). A conserved methionine was also mutated to alanine in the α L -α M chimera ( C ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated α L constructs plus β 2 -D709A and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. Data are presented as the MFI of the ICAM-1 binding normalized to integrin expression and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras or their mutants to α L -WT under the GFP-TH condition, or as indicated (*P
    Figure Legend Snippet: A conserved tyrosine residue within the MD regions of α X , α M , and α D negatively regulates TH-induced integrin activation. ( A–C) TH-induced ICAM-1 binding. The relatively conserved tyrosine was mutated to phenylalanine in all α L -chimeras ( A – C ), and to glutamic acid or alanine in the α L -α M chimera ( C ). A conserved methionine was also mutated to alanine in the α L -α M chimera ( C ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated α L constructs plus β 2 -D709A and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. Data are presented as the MFI of the ICAM-1 binding normalized to integrin expression and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras or their mutants to α L -WT under the GFP-TH condition, or as indicated (*P

    Techniques Used: Activation Assay, Binding Assay, Flow Cytometry, Transfection, Construct, Expressing, Two Tailed Test

    Integrin α L -chimeras bearing the α X , α D or α M CTMD regions show lower levels of TH-induced integrin activation than α L -WT. ( A) Representative overlaid flow cytometry plots of ICAM-1 binding, α L and GFP-TH expression in the log scale. HEK293FT cells were co-transfected with the indicated α L -chimeras and β 2 -D709A mutant plus GFP (plots not shown) or GFP-TH. The integrin and GFP-TH double-positive cells were gated for plotting the ICAM-1 binding and the expression of integrin and GFP-TH. (B) TH-induced ICAM-1 binding (quantitative data of A). Integrin and GFP-TH expression were presented in MFI in the lower panel. (C) ICAM-1 binding of α L -WT and α L -α M chimera in response to the different levels of GFP-TH expression. α L integrins were co-transfected with β 2 -D709A and the indicated amounts of GFP-TH plasmids into HEK293FT cells. For B and C, data are presented as the ICAM-1 MFI normalized to α L MFI and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras with α L -WT in the presence of GFP-TH in B or under same GFP-TH concentration in C. *P
    Figure Legend Snippet: Integrin α L -chimeras bearing the α X , α D or α M CTMD regions show lower levels of TH-induced integrin activation than α L -WT. ( A) Representative overlaid flow cytometry plots of ICAM-1 binding, α L and GFP-TH expression in the log scale. HEK293FT cells were co-transfected with the indicated α L -chimeras and β 2 -D709A mutant plus GFP (plots not shown) or GFP-TH. The integrin and GFP-TH double-positive cells were gated for plotting the ICAM-1 binding and the expression of integrin and GFP-TH. (B) TH-induced ICAM-1 binding (quantitative data of A). Integrin and GFP-TH expression were presented in MFI in the lower panel. (C) ICAM-1 binding of α L -WT and α L -α M chimera in response to the different levels of GFP-TH expression. α L integrins were co-transfected with β 2 -D709A and the indicated amounts of GFP-TH plasmids into HEK293FT cells. For B and C, data are presented as the ICAM-1 MFI normalized to α L MFI and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras with α L -WT in the presence of GFP-TH in B or under same GFP-TH concentration in C. *P

    Techniques Used: Activation Assay, Flow Cytometry, Binding Assay, Expressing, Transfection, Mutagenesis, Two Tailed Test, Concentration Assay

    The position of a tyrosine mutation at the α L CTMD region determines its negative effect on α L integrin inside-out activation. ( A ) Tyrosine mutations introduced into the α L CTMD region. ( B , D - E ) TH-induced ICAM-1 binding of the α L tyrosine mutations co-expressed with the β 2 -D709A mutant ( B , D ) or β 2 -WT ( E ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated integrin constructs and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. ICAM-1 binding is presented as the MFI of ICAM-1 normalized to integrin expression, and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L mutants to α L -WT under GFP-TH condition, or as indicated. *P
    Figure Legend Snippet: The position of a tyrosine mutation at the α L CTMD region determines its negative effect on α L integrin inside-out activation. ( A ) Tyrosine mutations introduced into the α L CTMD region. ( B , D - E ) TH-induced ICAM-1 binding of the α L tyrosine mutations co-expressed with the β 2 -D709A mutant ( B , D ) or β 2 -WT ( E ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated integrin constructs and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. ICAM-1 binding is presented as the MFI of ICAM-1 normalized to integrin expression, and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L mutants to α L -WT under GFP-TH condition, or as indicated. *P

    Techniques Used: Mutagenesis, Activation Assay, Binding Assay, Flow Cytometry, Transfection, Construct, Expressing, Two Tailed Test

    Related Articles

    Concentration Assay:

    Article Title: The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation
    Article Snippet: .. The concentration of ICAM-1-Fc in the supernatant was determined by ELISA using the anti-human ICAM-1 mAb (SinoBiological, Inc.) and the peroxidase-conjugated anti-human IgG1 (Fc specific) (Jackson ImmunoResearch Laboratories, Inc.). .. The culture supernatant was used for the ICAM-1 binding assay.

    Enzyme-linked Immunosorbent Assay:

    Article Title: The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation
    Article Snippet: .. The concentration of ICAM-1-Fc in the supernatant was determined by ELISA using the anti-human ICAM-1 mAb (SinoBiological, Inc.) and the peroxidase-conjugated anti-human IgG1 (Fc specific) (Jackson ImmunoResearch Laboratories, Inc.). .. The culture supernatant was used for the ICAM-1 binding assay.

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    Sino Biological anti human icam 1 mab
    A conserved tyrosine residue within the MD regions of α X , α M , and α D negatively regulates TH-induced integrin activation. ( A–C) TH-induced <t>ICAM-1</t> binding. The relatively conserved tyrosine was mutated to phenylalanine in all α L -chimeras ( A – C ), and to glutamic acid or alanine in the α L -α M chimera ( C ). A conserved methionine was also mutated to alanine in the α L -α M chimera ( C ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated α L constructs plus β 2 -D709A and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. Data are presented as the MFI of the ICAM-1 binding normalized to integrin expression and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras or their mutants to α L -WT under the GFP-TH condition, or as indicated (*P
    Anti Human Icam 1 Mab, supplied by Sino Biological, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti human icam 1 mab/product/Sino Biological
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti human icam 1 mab - by Bioz Stars, 2021-04
    91/100 stars
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    A conserved tyrosine residue within the MD regions of α X , α M , and α D negatively regulates TH-induced integrin activation. ( A–C) TH-induced ICAM-1 binding. The relatively conserved tyrosine was mutated to phenylalanine in all α L -chimeras ( A – C ), and to glutamic acid or alanine in the α L -α M chimera ( C ). A conserved methionine was also mutated to alanine in the α L -α M chimera ( C ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated α L constructs plus β 2 -D709A and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. Data are presented as the MFI of the ICAM-1 binding normalized to integrin expression and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras or their mutants to α L -WT under the GFP-TH condition, or as indicated (*P

    Journal: Scientific Reports

    Article Title: The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation

    doi: 10.1038/s41598-018-23444-w

    Figure Lengend Snippet: A conserved tyrosine residue within the MD regions of α X , α M , and α D negatively regulates TH-induced integrin activation. ( A–C) TH-induced ICAM-1 binding. The relatively conserved tyrosine was mutated to phenylalanine in all α L -chimeras ( A – C ), and to glutamic acid or alanine in the α L -α M chimera ( C ). A conserved methionine was also mutated to alanine in the α L -α M chimera ( C ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated α L constructs plus β 2 -D709A and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. Data are presented as the MFI of the ICAM-1 binding normalized to integrin expression and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras or their mutants to α L -WT under the GFP-TH condition, or as indicated (*P

    Article Snippet: The concentration of ICAM-1-Fc in the supernatant was determined by ELISA using the anti-human ICAM-1 mAb (SinoBiological, Inc.) and the peroxidase-conjugated anti-human IgG1 (Fc specific) (Jackson ImmunoResearch Laboratories, Inc.).

    Techniques: Activation Assay, Binding Assay, Flow Cytometry, Transfection, Construct, Expressing, Two Tailed Test

    Integrin α L -chimeras bearing the α X , α D or α M CTMD regions show lower levels of TH-induced integrin activation than α L -WT. ( A) Representative overlaid flow cytometry plots of ICAM-1 binding, α L and GFP-TH expression in the log scale. HEK293FT cells were co-transfected with the indicated α L -chimeras and β 2 -D709A mutant plus GFP (plots not shown) or GFP-TH. The integrin and GFP-TH double-positive cells were gated for plotting the ICAM-1 binding and the expression of integrin and GFP-TH. (B) TH-induced ICAM-1 binding (quantitative data of A). Integrin and GFP-TH expression were presented in MFI in the lower panel. (C) ICAM-1 binding of α L -WT and α L -α M chimera in response to the different levels of GFP-TH expression. α L integrins were co-transfected with β 2 -D709A and the indicated amounts of GFP-TH plasmids into HEK293FT cells. For B and C, data are presented as the ICAM-1 MFI normalized to α L MFI and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras with α L -WT in the presence of GFP-TH in B or under same GFP-TH concentration in C. *P

    Journal: Scientific Reports

    Article Title: The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation

    doi: 10.1038/s41598-018-23444-w

    Figure Lengend Snippet: Integrin α L -chimeras bearing the α X , α D or α M CTMD regions show lower levels of TH-induced integrin activation than α L -WT. ( A) Representative overlaid flow cytometry plots of ICAM-1 binding, α L and GFP-TH expression in the log scale. HEK293FT cells were co-transfected with the indicated α L -chimeras and β 2 -D709A mutant plus GFP (plots not shown) or GFP-TH. The integrin and GFP-TH double-positive cells were gated for plotting the ICAM-1 binding and the expression of integrin and GFP-TH. (B) TH-induced ICAM-1 binding (quantitative data of A). Integrin and GFP-TH expression were presented in MFI in the lower panel. (C) ICAM-1 binding of α L -WT and α L -α M chimera in response to the different levels of GFP-TH expression. α L integrins were co-transfected with β 2 -D709A and the indicated amounts of GFP-TH plasmids into HEK293FT cells. For B and C, data are presented as the ICAM-1 MFI normalized to α L MFI and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L -chimeras with α L -WT in the presence of GFP-TH in B or under same GFP-TH concentration in C. *P

    Article Snippet: The concentration of ICAM-1-Fc in the supernatant was determined by ELISA using the anti-human ICAM-1 mAb (SinoBiological, Inc.) and the peroxidase-conjugated anti-human IgG1 (Fc specific) (Jackson ImmunoResearch Laboratories, Inc.).

    Techniques: Activation Assay, Flow Cytometry, Binding Assay, Expressing, Transfection, Mutagenesis, Two Tailed Test, Concentration Assay

    The position of a tyrosine mutation at the α L CTMD region determines its negative effect on α L integrin inside-out activation. ( A ) Tyrosine mutations introduced into the α L CTMD region. ( B , D - E ) TH-induced ICAM-1 binding of the α L tyrosine mutations co-expressed with the β 2 -D709A mutant ( B , D ) or β 2 -WT ( E ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated integrin constructs and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. ICAM-1 binding is presented as the MFI of ICAM-1 normalized to integrin expression, and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L mutants to α L -WT under GFP-TH condition, or as indicated. *P

    Journal: Scientific Reports

    Article Title: The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation

    doi: 10.1038/s41598-018-23444-w

    Figure Lengend Snippet: The position of a tyrosine mutation at the α L CTMD region determines its negative effect on α L integrin inside-out activation. ( A ) Tyrosine mutations introduced into the α L CTMD region. ( B , D - E ) TH-induced ICAM-1 binding of the α L tyrosine mutations co-expressed with the β 2 -D709A mutant ( B , D ) or β 2 -WT ( E ). Binding of ICAM-1 was measured by flow cytometry with HEK293FT cells co-transfected with the indicated integrin constructs and GFP or GFP-TH. The GFP and integrin double-positive cells were analyzed. ICAM-1 binding is presented as the MFI of ICAM-1 normalized to integrin expression, and shown as mean ± s.e.m. (n ≥ 3). Two-tailed Student’s t-test was performed to compare the α L mutants to α L -WT under GFP-TH condition, or as indicated. *P

    Article Snippet: The concentration of ICAM-1-Fc in the supernatant was determined by ELISA using the anti-human ICAM-1 mAb (SinoBiological, Inc.) and the peroxidase-conjugated anti-human IgG1 (Fc specific) (Jackson ImmunoResearch Laboratories, Inc.).

    Techniques: Mutagenesis, Activation Assay, Binding Assay, Flow Cytometry, Transfection, Construct, Expressing, Two Tailed Test