Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
Submit
Validation data
Reference
Comment
Report error
- Product number
- ABIN968078 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Integrin, alpha 5 (Fibronectin Receptor, alpha Polypeptide) (ITGA5) (AA 853-1002) antibody
- Antibody type
- Monoclonal
- Antigen
- Human Integrin alpha5
- Description
- Purified from tissue culture supernatant or ascites by affinity chromatography.
- Reactivity
- Human
- Host
- Mouse
- Epitope
- AA 853-1002
- Isotype
- IgG
- Antibody clone number
- 1
- Vial size
- 150 μg
- Concentration
- 250 μg/ml
- Storage
- -20°C
Submitted references Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions.
Nischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migration.
Anchorage-dependent regulation of the mitogen-activated protein kinase cascade by growth factors is supported by a variety of integrin alpha chains.
Functional role of N-glycosylation in alpha 5 beta 1 integrin receptor. De-N-glycosylation induces dissociation or altered association of alpha 5 and beta 1 subunits and concomitant loss of fibronectin binding activity.
Functional role of the cytoplasmic domain of the integrin alpha 5 subunit.
Sottile J, Hocking DC
Molecular biology of the cell 2002 Oct;13(10):3546-59
Molecular biology of the cell 2002 Oct;13(10):3546-59
Nischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migration.
Alahari SK, Lee JW, Juliano RL
The Journal of cell biology 2000 Dec 11;151(6):1141-54
The Journal of cell biology 2000 Dec 11;151(6):1141-54
Anchorage-dependent regulation of the mitogen-activated protein kinase cascade by growth factors is supported by a variety of integrin alpha chains.
Aplin AE, Short SM, Juliano RL
The Journal of biological chemistry 1999 Oct 29;274(44):31223-8
The Journal of biological chemistry 1999 Oct 29;274(44):31223-8
Functional role of N-glycosylation in alpha 5 beta 1 integrin receptor. De-N-glycosylation induces dissociation or altered association of alpha 5 and beta 1 subunits and concomitant loss of fibronectin binding activity.
Zheng M, Fang H, Hakomori S
The Journal of biological chemistry 1994 Apr 22;269(16):12325-31
The Journal of biological chemistry 1994 Apr 22;269(16):12325-31
Functional role of the cytoplasmic domain of the integrin alpha 5 subunit.
Bauer JS, Varner J, Schreiner C, Kornberg L, Nicholas R, Juliano RL
The Journal of cell biology 1993 Jul;122(1):209-21
The Journal of cell biology 1993 Jul;122(1):209-21
No comments: Submit comment
No validations: Submit validation data