Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations
- Flow cytometry [1]
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- Product number
- ABIN2472753 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Fc Fragment of IgA, Receptor For (FCAR) antibody
- Antibody type
- Monoclonal
- Description
- Purified
- Reactivity
- Human
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- MIP8a
- Vial size
- 0.2 mg
Submitted references Recognition and functional activation of the human IgA receptor (FcalphaRI) by C-reactive protein.
Antigen binding to secretory immunoglobulin A results in decreased sensitivity to intestinal proteases and increased binding to cellular Fc receptors.
Neutrophil lactoferrin release induced by IgA immune complexes differed from that induced by cross-linking of fcalpha receptors (FcalphaR) with a monoclonal antibody, MIP8a.
Structural aspects of the membrane of the endoplasmic reticulum.
Lu J, Marjon KD, Marnell LL, Wang R, Mold C, Du Clos TW, Sun P
Proceedings of the National Academy of Sciences of the United States of America 2011 Mar 22;108(12):4974-9
Proceedings of the National Academy of Sciences of the United States of America 2011 Mar 22;108(12):4974-9
Antigen binding to secretory immunoglobulin A results in decreased sensitivity to intestinal proteases and increased binding to cellular Fc receptors.
Duc M, Johansen FE, Corthésy B
The Journal of biological chemistry 2010 Jan 8;285(2):953-60
The Journal of biological chemistry 2010 Jan 8;285(2):953-60
Neutrophil lactoferrin release induced by IgA immune complexes differed from that induced by cross-linking of fcalpha receptors (FcalphaR) with a monoclonal antibody, MIP8a.
Zhang W, Bi B, Oldroyd RG, Lachmann PJ
Clinical and experimental immunology 2000 Jul;121(1):106-11
Clinical and experimental immunology 2000 Jul;121(1):106-11
Structural aspects of the membrane of the endoplasmic reticulum.
Depierre JW, Dallner G
Biochimica et biophysica acta 1975 Dec 29;415(4):411-72
Biochimica et biophysica acta 1975 Dec 29;415(4):411-72
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