Alpha-Dystroglycan1, Abcam, ab234587

Abcam ab234587 · Alpha-Dystroglycan1 · Recombinant
2.76
(Overall rating from 1 review)
#2 of 3 targeting Alpha-Dystroglycan1
2.76
From 1 review · #2 of 3 for Alpha-Dystroglycan1

Information about this antibody

Vendor
Catalog No
ab234587
Application
N/A
Clonality
Recombinant
Origin
N/A
Reactivity
N/A
Conjugation
N/A
Product Link
N/A
Clone ID
IIH6 C4

Vendor notes

No vendor notes available for this antibody.

pAbmAbs Average Ratings

ℹ
Western Blot
3.77
IP
1.70
Overall
2.76
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User Reviews (1)

Review of: Alpha-Dystroglycan1, Abcam, ab234587 by pAbmAbs Data Mining

Reviewed: May 8, 2026

Our team has carried out deep research in the published scientific literature to identify papers and reports using antibodies directed against human Dystroglycan 1 and followed up by extraction and evaluation of the available data to assess its performance according to pAbmAbs rating criteria.

YCharOS is here conducting a large head-to-head study comparing 14 commercial research antibodies against human Dystroglycan 1encoded by DAG1. Dystroglycan 1 is cleaved into the following 2 chains: Alpha-dystroglycan and Beta-dystroglycan. The antibodies tested has specificity for either one of the chains or both.

The collection of antibodies against Beta-dystroglycan was tested using A431WT and DAG1 KO cells in the applications WB (WT and KO cell lysates/90 µg protein) and IF (WT and KO cells), according to YCharOS standard protocols (see reference).

The collection of antibodies against Alfa-dystroglycan was tested using HAP1 WT and DAG1 KO cells in the applications WB (WT and KO cell lysates/100 µg protein) and IP (WT cell lysate), according to YCharOS standard protocols (see reference).

ab234587 has specificity for Alpha-Dystroglycan. In WB (1:500 Ab dilution) ab234587 detected a faint band of appr. 120 kDa in HAP1 WT culture media, with no corresponding band observed in HAP1 KO culture media. Several bands of strong intensity were observed following IP (2 µg Ab used) from HAP1 cell lysate. The intensity of these bands was comparable to that of the corresponding band in the input extract (10% of starting material). A strong band was also detected in immunodepleted extract (10% of total unbound fraction), showing that the antibody does not completely deplete the antigen from the cell lysate.

We highly encourage other scientists to share their observations.

Western Blot
IP

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