Alpha-1-antitrypsin, Human, mAb 2C1 - HM2289-20UG
Catalog #
HM2289-20UG
125,00 €
The mouse monoclonal antibody clone 2C1 recognizes polymeric forms of human alpha-1-antitrypsin.
Alpha-1-antitrypsin is the most abundant circulating protease inhibitor. Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serine protease inhibitor or serpin superfamily of proteins.1
The best known is a1-antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). The severe Z deficiency allele (Glu342Lys) causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. This causes neonatal hepatitis, cirrhosis, and hepatocellular carcinoma.
Clone 2C1 recognizes polymers formed by Z α1-antitrypsin in vivo. It also recognizes polymers formed by the Siiyama (Ser53Phe) and Brescia (Gly225Arg) mutants, and the novel His334Asp shutter domain mutant of a1-antitrypsin that is associated with prolonged neonatal jaundice in a 6-week-old boy. These data show that Z and shutter domain mutants form polymers with a shared epitope.
| Datasheet URL | https://www.hycultbiotech.com/wp-content/uploads/2023/05/SDS-HM2289-100UG.pdf |
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| Quantity | 20 µg |
| Species | Human |
| Alias | Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Serpin A1, A1AT Gene name: SERPINA1 |
| Application | Immuno assays, Immuno fluorescence, Immuno precipitation, Paraffin sections, Western blot |
| Precautions | For research use only. Not for use in or on humans or animals or for diagnostics. It is the responsibility of the user to comply with all local/state and federal rules in the use of this product. Hycult Biotech is not responsible for any patent infringements that might result from the use or derivation of this product. |
| References | 1. Miranda, E et al; A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency. Hepatology 2010, 52: 1078. 2. Ekeowa, U et al; Defining the mechanism of polymerization in the serpinopathies. PNAS 2010, 107: 17146. 3. Morris, H et al; ANCA-associated vasculitis is linked to carriage of the Z allele of α1 antitrypsin and its polymers. Ann Rheum Dis 2011, 70: 1851. 4. Yamasaki, M et al; Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO reports 2011, 12: 1011. 5. Ordonez, A et al; A single-chain variable fragment intrabody prevents intracellular polymerization of Z a1-antitrypsin while allowing its antiproteinase activity. FASEB Journal 2015, 29: 2667 6. Tan, L et al; Characterising the association of latency with α1-antitrypsin polymerisation using a novel monoclonal antibody. Int J Bio & Cell Biol 2015, 58: 81 7. Dickens, J et al; The endoplasmic reticulum remains functionally connected by vesicular transport after its fragmentation in cells expressing Z-a1-antitrypsin. FASEB Journal 2016, 30: 4083 8. Haq, I et al; Deficiency Mutations of Alpha-1 Antitrypsin. Am J Respir Cell Mol Biol 2016, 1: 71 9. Khodayari, N et al; Erdj3 Has an Essential Role for Z Variant Alpha-1-Antitrypsin Degradation. J Cell Bio 2017, 118: 3090 10. Miranda, E et al; The pathological Trento variant of alpha-1-antitrypsin (E75V) shows nonclassical behaviour during polymerization. FEBS Journal 2017, 284: 2110 |
| Disease | Autoimmunity, Pulmonology |
| Application: | Immuno assays Immuno fluorescence Immuno precipitation Paraffin sections Western blot |
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