These mouse IgG2a monoclonal antibodies was generated against his-tagged protein and recognize human and mouse endoplasmic reticulum (ER) protein 57.
These antibodies were raised against ERp57, which is an isomerase enzyme that has protein disulfide isomerase activity. This protein localizes to the endoplasmic reticulum (ER) and interacts with lectin chaperones calreticulin and calnexin (CNX) to modulate folding of newly synthesized glycoproteins. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. The function of ERp57 involves immunity, regulation of oxidative stress, cell adhesion, growth signaling and death, as well as thrombosis.
From the laboratory of David W. Essex, MD, Temple University.
|Antigen:||Full length human ERp57|
|Molecular Weight:||57 kDa|
|Reactivity:||Human and Mouse|
|Buffer:||0.1M Sodium Phosphate, pH 7.4, 0.15M NaCl, 0.05% (w/v) Sodium Azide|
|Tested Applications:||WB, flow cytometry, inhibition of platelet aggregation|
|Comments:||The Abs were screened for inhibition of platelet aggregation, and an IgG2a Ab (3G1, herein called Mab1) was found that inhibited platelet aggregation. Another IgG2a Ab (1B12, herein called Mab2) reacted with ERp57 by Western blot but did not inhibit platelet aggregation. This Ab was used as a control and compared with the isotype-specific IgG2a control Ab.|
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