l1cam polyclonal antibody Search Results


94
R&D Systems goat polyclonal anti chl1
Goat Polyclonal Anti Chl1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
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Bioss l1cam biotinylated antibody
L1cam Biotinylated Antibody, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
l1cam biotinylated antibody - by Bioz Stars, 2026-03
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90
Santa Cruz Biotechnology rabbit polyclonal anti-l1cam
Rabbit Polyclonal Anti L1cam, supplied by Santa Cruz Biotechnology, 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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Average 90 stars, based on 1 article reviews
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93
Proteintech l1cam rabbit polyclonal antibody
Western blot analysis was conducted to assess the expression of neural protein markers in the brains of Balb/c mice treated with PLGA-EVG (25 mg/kg) and PLGA-CUR (20 mg/kg). Proteins were extracted from brain tissue and analyzed for the expression of ( a ) <t>L1CAM,</t> ( b ) NeuN, ( c ) GFAP, and ( d ) synaptophysin. Data are presented as means ± S.E.M ( n = 4). Statistical comparisons among groups were performed using one-way ANOVA followed by Tukey’s post hoc test.
L1cam Rabbit Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/l1cam rabbit polyclonal antibody/product/Proteintech
Average 93 stars, based on 1 article reviews
l1cam rabbit polyclonal antibody - by Bioz Stars, 2026-03
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90
R&D Systems anti l1cam
Western blot analysis was conducted to assess the expression of neural protein markers in the brains of Balb/c mice treated with PLGA-EVG (25 mg/kg) and PLGA-CUR (20 mg/kg). Proteins were extracted from brain tissue and analyzed for the expression of ( a ) <t>L1CAM,</t> ( b ) NeuN, ( c ) GFAP, and ( d ) synaptophysin. Data are presented as means ± S.E.M ( n = 4). Statistical comparisons among groups were performed using one-way ANOVA followed by Tukey’s post hoc test.
Anti L1cam, supplied by R&D Systems, 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/anti l1cam/product/R&D Systems
Average 90 stars, based on 1 article reviews
anti l1cam - by Bioz Stars, 2026-03
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93
Santa Cruz Biotechnology goat anti l1cam polyclonal antibody
Associations between <t> L1CAM </t> protein and clinicopathological characteristics of patients with breast cancer
Goat Anti L1cam Polyclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/goat anti l1cam polyclonal antibody/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
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Santa Cruz Biotechnology anti-neural cell adhesion molecule l1 cytoplasmic domain (anti-l1cd)
Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat <t>polyclonal</t> antibody to <t>L1CD</t> or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) <t>L1</t> (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.
Anti Neural Cell Adhesion Molecule L1 Cytoplasmic Domain (Anti L1cd), supplied by Santa Cruz Biotechnology, 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/anti-neural cell adhesion molecule l1 cytoplasmic domain (anti-l1cd)/product/Santa Cruz Biotechnology
Average 90 stars, based on 1 article reviews
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92
R&D Systems af2126
Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat <t>polyclonal</t> antibody to <t>L1CD</t> or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) <t>L1</t> (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.
Af2126, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
R&D Systems goat anti human
Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat <t>polyclonal</t> antibody to <t>L1CD</t> or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) <t>L1</t> (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.
Goat Anti Human, supplied by R&D Systems, 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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93
R&D Systems bsa in pbs
Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat <t>polyclonal</t> antibody to <t>L1CD</t> or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) <t>L1</t> (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.
Bsa In Pbs, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Thermo Fisher rabbit polyclonal antibody l1cam 13-1719-82
Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat <t>polyclonal</t> antibody to <t>L1CD</t> or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) <t>L1</t> (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.
Rabbit Polyclonal Antibody L1cam 13 1719 82, 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
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Average 90 stars, based on 1 article reviews
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Image Search Results


Western blot analysis was conducted to assess the expression of neural protein markers in the brains of Balb/c mice treated with PLGA-EVG (25 mg/kg) and PLGA-CUR (20 mg/kg). Proteins were extracted from brain tissue and analyzed for the expression of ( a ) L1CAM, ( b ) NeuN, ( c ) GFAP, and ( d ) synaptophysin. Data are presented as means ± S.E.M ( n = 4). Statistical comparisons among groups were performed using one-way ANOVA followed by Tukey’s post hoc test.

Journal: Brain Sciences

Article Title: PLGA-Encapsulated Elvitegravir and Curcumin Modulates ART Penetration, Oxidative Stress, and Inflammation

doi: 10.3390/brainsci15040328

Figure Lengend Snippet: Western blot analysis was conducted to assess the expression of neural protein markers in the brains of Balb/c mice treated with PLGA-EVG (25 mg/kg) and PLGA-CUR (20 mg/kg). Proteins were extracted from brain tissue and analyzed for the expression of ( a ) L1CAM, ( b ) NeuN, ( c ) GFAP, and ( d ) synaptophysin. Data are presented as means ± S.E.M ( n = 4). Statistical comparisons among groups were performed using one-way ANOVA followed by Tukey’s post hoc test.

Article Snippet: The antibodies included NeuN rabbit polyclonal antibody (1:1000, 26975-1-AP, Proteintech Inc, (Rosemont, IL, USA)), synaptophysin mouse monoclonal antibody (1:20,000, 67864-1-Ig, Proteintech Inc, (Rosemont, IL, USA)), β-actin mouse monoclonal antibody (1:20,000, 66009-1-Ig, Proteintech Inc, (Rosemont, IL, USA)), GFAP rabbit polyclonal antibody (1:1000), and L1CAM rabbit polyclonal antibody (catalog no. 20659-1-AP, Proteintech Inc, Rosemont, IL, USA).

Techniques: Western Blot, Expressing

Associations between  L1CAM  protein and clinicopathological characteristics of patients with breast cancer

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Overexpression of L1 cell adhesion molecule correlates with aggressive tumor progression of patients with breast cancer and promotes motility of breast cancer cells

doi:

Figure Lengend Snippet: Associations between L1CAM protein and clinicopathological characteristics of patients with breast cancer

Article Snippet: After blocking with 5% non-fat milk, the membranes were probed with goat anti-L1CAM polyclonal antibody (#sc-31032, Santa Cruz Biotechnology, CA, USA).

Techniques: Expressing

Overexpression of L1CAM protein in human breast cancer tissues. A. Positive L1CAM immunostaining was localized in the membrane of breast cancer cells; B. Negative or weak membrane staining of L1CAM was shown in non-cancerous breast tissues; C. There were 88 of 100 (88.0%) cases of breast cancer overexpressed L1CAM compared with the matched non-cancerous breast tissues; D. Statistical analysis showed that the L1CAM expression level in breast cancer tissues was higher than that in the matched non-cancerous breast tissues, with mean IRS at 5.12 ± 1.19 vs. 3.08 ± 0.84 (P<0.05).

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Overexpression of L1 cell adhesion molecule correlates with aggressive tumor progression of patients with breast cancer and promotes motility of breast cancer cells

doi:

Figure Lengend Snippet: Overexpression of L1CAM protein in human breast cancer tissues. A. Positive L1CAM immunostaining was localized in the membrane of breast cancer cells; B. Negative or weak membrane staining of L1CAM was shown in non-cancerous breast tissues; C. There were 88 of 100 (88.0%) cases of breast cancer overexpressed L1CAM compared with the matched non-cancerous breast tissues; D. Statistical analysis showed that the L1CAM expression level in breast cancer tissues was higher than that in the matched non-cancerous breast tissues, with mean IRS at 5.12 ± 1.19 vs. 3.08 ± 0.84 (P<0.05).

Article Snippet: After blocking with 5% non-fat milk, the membranes were probed with goat anti-L1CAM polyclonal antibody (#sc-31032, Santa Cruz Biotechnology, CA, USA).

Techniques: Over Expression, Immunostaining, Membrane, Staining, Expressing

RNA interference-mediated knockdown of L1CAM protein in breast cancer cells in vitro. A. L1CAM protein levels in nontargeting control siRNA (si-con) and L1CAM-targeting siRNA (si-L1CAM) transfected HBL-100 and MCF-7 cells cells were detected by Western blot. B. LKB1 knockdown efficiency was quantified using densitometry. The L1CAM siRNA used in this study could reduce the level of L1CAM protein expression by >70% in both HBL-100 and MCF-7 cells.

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Overexpression of L1 cell adhesion molecule correlates with aggressive tumor progression of patients with breast cancer and promotes motility of breast cancer cells

doi:

Figure Lengend Snippet: RNA interference-mediated knockdown of L1CAM protein in breast cancer cells in vitro. A. L1CAM protein levels in nontargeting control siRNA (si-con) and L1CAM-targeting siRNA (si-L1CAM) transfected HBL-100 and MCF-7 cells cells were detected by Western blot. B. LKB1 knockdown efficiency was quantified using densitometry. The L1CAM siRNA used in this study could reduce the level of L1CAM protein expression by >70% in both HBL-100 and MCF-7 cells.

Article Snippet: After blocking with 5% non-fat milk, the membranes were probed with goat anti-L1CAM polyclonal antibody (#sc-31032, Santa Cruz Biotechnology, CA, USA).

Techniques: Knockdown, In Vitro, Control, Transfection, Western Blot, Expressing

Knockdown of L1CAM expression inhibits cellular motility of breast cancer cells in vitro. L1CAM knock-down HBL-100 and MCF-7 cells both showed an approximately 2.5-fold decrease in migration (A) and a 2-fold decrease in invasion (B), compared with L1CAM-overexpressing cells.

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Overexpression of L1 cell adhesion molecule correlates with aggressive tumor progression of patients with breast cancer and promotes motility of breast cancer cells

doi:

Figure Lengend Snippet: Knockdown of L1CAM expression inhibits cellular motility of breast cancer cells in vitro. L1CAM knock-down HBL-100 and MCF-7 cells both showed an approximately 2.5-fold decrease in migration (A) and a 2-fold decrease in invasion (B), compared with L1CAM-overexpressing cells.

Article Snippet: After blocking with 5% non-fat milk, the membranes were probed with goat anti-L1CAM polyclonal antibody (#sc-31032, Santa Cruz Biotechnology, CA, USA).

Techniques: Knockdown, Expressing, In Vitro, Migration

Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat polyclonal antibody to L1CD or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) L1 (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.

Journal: Birth defects research

Article Title: CHOLINE AMELIORATES ETHANOL INDUCED ALTERATIONS IN TYROSINE PHOSPHORYLATION AND DISTRIBUTION IN DETERGENT-RESISTANT MEMBRANE MICRODOMAINS OF L1 CELL ADHESION MOLECULE IN VIVO

doi: 10.1002/bdr2.1657

Figure Lengend Snippet: Immunoprecipitation of lysates from each of the 3 control pups were performed using either goat polyclonal antibody to L1CD or goat IgG. Immunoprecipitants were blotted for either A) phosphotyrosine (PY100) or B) L1 (using antibody to L1CD). The immunoblot with PY100 (A) shows only the 220 kD and 80 kD bands consistent with L1. The immunoblot for L1 (B) only shows the heavy chain of the goat IgG from the immunoprecipiatation at 50 kD in addition to the 220 kD and 80 kD bands for L1 when the secondary antibody was donkey anti-goat IgG.

Article Snippet: Goat polyclonal anti-neural cell adhesion molecule L1 cytoplasmic domain (anti-L1CD) was from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

Techniques: Immunoprecipitation, Control, Western Blot