Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- ABIN968131 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Amphiphysin (AMPH) (AA 258-414) antibody
- Antibody type
- Monoclonal
- Antigen
- Human Amphiphysin
- Description
- Purified from tissue culture supernatant or ascites by affinity chromatography.
- Reactivity
- Human
- Host
- Mouse
- Epitope
- AA 258-414
- Isotype
- IgG
- Antibody clone number
- Ghr5
- Vial size
- 50 μg
- Concentration
- 250 μg/ml
- Storage
- -20°C
Submitted references Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller.
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.
The appendage domain of alpha-adaptin is a high affinity binding site for dynamin.
Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161.
Drake MT, Traub LM
The Journal of biological chemistry 2001 Aug 3;276(31):28700-9
The Journal of biological chemistry 2001 Aug 3;276(31):28700-9
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.
Traub LM, Downs MA, Westrich JL, Fremont DH
Proceedings of the National Academy of Sciences of the United States of America 1999 Aug 3;96(16):8907-12
Proceedings of the National Academy of Sciences of the United States of America 1999 Aug 3;96(16):8907-12
The appendage domain of alpha-adaptin is a high affinity binding site for dynamin.
Wang LH, Südhof TC, Anderson RG
The Journal of biological chemistry 1995 Apr 28;270(17):10079-83
The Journal of biological chemistry 1995 Apr 28;270(17):10079-83
Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161.
David C, Solimena M, De Camilli P
FEBS letters 1994 Aug 29;351(1):73-9
FEBS letters 1994 Aug 29;351(1):73-9
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