Key Specifications Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H||ICC, NEUT||M||Purified||Monoclonal Antibody|
|Description||Anti-Integrin α1 Antibody, clone 5E8D9|
|Presentation||0.1M Tris-glycine, pH 7.4, 0.15M NaCl|
|Application||Anti-Integrin α1 Antibody, clone 5E8D9 is an antibody against Integrin α1 for use in IC, NEUT.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||2 years at -20°C|
|Material Size||200 µg|
|Reference overview||Application||Pub Med ID|
|Enhancement of cell adhesion and spreading by a cartilage-specific noncollagenous protein, cartilage matrix protein (CMP/Matrilin-1), via integrin alpha1beta1 |
Makihira, S., et al
J Biol Chem, 274:11417-23 (1999) 1999
|Pro-adhesive and chemotactic activities of thrombospondin-1 for breast carcinoma cells are mediated by alpha3beta1 integrin and regulated by insulin-like growth factor-1 and CD98. |
S Chandrasekaran, N H Guo, R G Rodrigues, J Kaiser, D D Roberts
The Journal of biological chemistry 274 11408-16 1999
Thrombospondin-1 (TSP1) is a matricellular protein that displays both pro- and anti-adhesive activities. Binding to sulfated glycoconjugates mediates most high affinity binding of soluble TSP1 to MDA-MB-435 cells, but attachment and spreading of these cells on immobilized TSP1 is primarily beta1 integrin-dependent. The integrin alpha3beta1 is the major mediator of breast carcinoma cell adhesion and chemotaxis to TSP1. This integrin is partially active in MDA-MB-435 cells but is mostly inactive in MDA-MB-231 and MCF-7 cells, which require beta1 integrin activation to induce spreading on TSP1. Integrin-mediated cell spreading on TSP1 is accompanied by extension of filopodia containing beta1 integrins. TSP1 binding activity of the alpha3beta1 integrin is not stimulated by CD47-binding peptides from TSP1 or by protein kinase C activation, which activate alphavbeta3 integrin function in the same cells. In MDA-MB-231 but not MDA-MB-435 cells, this integrin is activated by pertussis toxin, whereas serum, insulin, insulin-like growth factor-1, and ligation of CD98 increase activity of this integrin in both cell lines. Serum stimulation is accompanied by increased surface expression of CD98, whereas insulin-like growth factor-1 does not increase CD98 expression. Thus, the pro-adhesive activity of TSP1 for breast carcinoma cells is controlled by several signals that regulate activity of the alpha3beta1 integrin.
|Immunofluorescence, Flow Cytometry||10196234|
|The integrin alpha1 A-domain is a ligand binding site for collagens and laminin |
Calderwood, D. A., et al
J Biol Chem, 272:12311-7 (1997) 1997
|Regulation of polymorphonuclear leukocyte cytokine receptor expression: the role of altered oxygen tensions and matrix proteins |
Simms, H. and D'Amico, R.
J Immunol, 157:3605-16 (1996) 1996
|Functional regulation of the human integrin VLA-1 (CD49a/CD29) by divalent cations and stimulatory beta 1 antibodies. |
Luque, A, et al.
FEBS Lett., 346: 278-84 (1994) 1994
We have investigated the regulation by divalent cations Mg2+, Ca2+ and Mn2+ of the functional activity of the human integrin VLA-1 expressed on neuroblastoma NB100 cells. VLA-1-mediated adhesion of NB100 cells to ligand collagen type I was supported by either mM concentrations of extracellular Mg2+ or microM levels of Mn2+. In contrast, Ca2+ alone did not induce activation of VLA-1 but exerted a potent inhibitory effect on the Mg(2+)-supported cell adhesion. We have also demonstrated that VLA-1 can be directly activated by the stimulatory monoclonal antibody TS2/16 specific for the integrin beta 1 subunit, resulting in effective adhesion of NB100 cells to type I collagen. This study has been possible by using a novel blocking VLA-alpha 1 specific monoclonal antibody, 5E8D9.
|Regulation of the VLA integrin-ligand interactions through the beta 1 subunit. |
Arroyo, A G, et al.
J. Cell Biol., 117: 659-70 (1992) 1992