| + |
Laminin-10 | up-regulates activity 
binding
|
Laminin-10 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253277 |
|
|
Mus musculus |
Embryonic Stem Cell |
| pmid |
sentence |
| 18757303 |
Recombinant human LN-511 alone was suffi- cient to enable self-renewal of mouse ES cells for up to 169 days (31 passages). Cells cultured on LN-511 maintained expression of pluripotency markers, such as Oct4, Sox2, Tert, UTF1, and Nanog|ES cells interacted with LN-511 via 1-integrins, mostly a6b1 and aVb1. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
LAMB1 | form complex 
binding
|
Laminin-10 |
0.719 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253230 |
|
|
|
|
| pmid |
sentence |
| 11821406 |
The laminin (LN) family of large heterotrimeric extracellular matrix glycoproteins has multiple functions: LNs take part in the regulation of processes such as cell migration, differentiation, and proliferation, in addition to contributing to the structure of basement membranes. LN-10, composed of alpha5, beta1, and gamma1 chains, is widely distributed in most basement membranes of both epithelia and endothelia. |
|
| Publications: |
1 |
| + |
LAMC1 | form complex
binding
|
Laminin-10 |
0.704 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253231 |
|
|
|
|
| pmid |
sentence |
| 11821406 |
The laminin (LN) family of large heterotrimeric extracellular matrix glycoproteins has multiple functions: LNs take part in the regulation of processes such as cell migration, differentiation, and proliferation, in addition to contributing to the structure of basement membranes. LN-10, composed of alpha5, beta1, and gamma1 chains, is widely distributed in most basement membranes of both epithelia and endothelia. |
|
| Publications: |
1 |
| + |
Laminin-10 | up-regulates activity
binding
|
A6/b1 integrin |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253222 |
|
|
|
|
| pmid |
sentence |
| 12123670 |
We have developed a cell-free assay for binding of solubilized beta1 integrins to their physiologically relevant ligands using an electrochemiluminescent detection method|Binding was clearly optimal for the presumed physiological ligands, i.e., collagen IV for a1b1, collagen I for a2b1, VCAM-Ig for a4b1, fibronectin (the 120-kDa cell attachment fragment was used) for a5b1, and laminin for a6b1. |
|
| Publications: |
1 |
| + |
LAMA5 | form complex
binding
|
Laminin-10 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255317 |
|
|
|
|
| pmid |
sentence |
| 11821406 |
The laminin (LN) family of large heterotrimeric extracellular matrix glycoproteins has multiple functions: LNs take part in the regulation of processes such as cell migration, differentiation, and proliferation, in addition to contributing to the structure of basement membranes. LN-10, composed of alpha5, beta1, and gamma1 chains, is widely distributed in most basement membranes of both epithelia and endothelia. |
|
| Publications: |
1 |
3.0
Laminin-10
CPX-1779