iMatrix-411 Endothelial Cell Substrate

iMatrix-411 is a xeno-free, recombinant Laminin-411 E8 Fragment expressed in CHO-S cells. Laminin-411 is found predominantly in the vascular endothelial basement membrane. Stem cells cultivated on iMatrix-411 are robustly induced to differentiate into endothelial progenitor cells.

iMatrix-411 features make it an ideal matrix for some cell culture applications:

• Xeno-free formulation / CHO-S cell bioproduction
• Easy to use (liquid format)
• E8-fragments retain integrin binding specificity and capacity, and display higher potency than natural Laminin-411
• Cultivation of iPSC on iMatrix-411 induces a cell fate transition to endothelial progenitor cells

iMatrix-411 is a highly purified and refined product of human recombinant laminin-411 (E8 fragment) expressed by CHO-S cells. Laminin-411 is found predominantly expressed in the vascular endothelial basement membrane¹ and in Langerhans islet capillary endothelial cells of the pancreas.²

As a cell culture ECM-substrate iMatrix-411 can assist in establishing human endothelial cell primary cultures from fresh human bio-specimens.

Human iPS cells, when cultured on iMatrix-411, are robustly induced (>95%) to differentiate into endothelial progenitor cells with angiogenesis capacity.¹ Other published reports have used iMatrix-411 and iMatrix-511 in a step-wise protocol to generate cholangiocytes capable of forming 3D cyst-structures from iPSC-derived hepatoblastic cells.³

Matrixome company name and logo and iMatrix brand name are the property of Matrixome Corp., Japan.

Product Name: iMatrix-411 Endothelial Cell Substrate

Catalog Numbers:

• NP892-041
• NP892-042

Sizes:

• NP892-041: 2 × 175 µg
• NP892-042: 6 × 175 µg

Molecular Weight: 150 kDa

Purity: > 95 % pure

Formulation: Purified Laminin-411 E8 proteolytic fragment

Storage and Stability: Store at 4 °C and protect from light exposure. Stable for 2 years from manufacturing date.

Quality Control: Activity: K_d for integrin binding

Sterility: Sterile

Notice To Purchaser: REPROCELL is a licensed distributor of Matrixome cell culture substrates to the global market

Recommended Usage: iMatrix-411 is suitable for use as a substrate for culture of various cell types, but most notably for vascular endothelial cells.

Concentration: 500 µg/mL

Source: CHO-S cell expression

Manufacturer: Matrixome Corporation (Japan)

Safety Data Sheet:

• NP892-04 Safety Data Sheet

Product Flyer:

• iMatrix™ Cell Culture Substrates

1. Ohta R. et al., "Laminin-guided highly efficient endothelial commitment from human pluripotent stem cells". Scientific Reports 6:35680 / DOI: 10.1038/srep35680 (2016).
2. Lammert E.,Cleaver O.,Melton D., Mechanisms of Development (Elsevier)120 (1) 59-64 (2003).
3. Takayama K. et al., "Laminin 411 and 511 promote the cholangiocyte differentiation of human induced pluripotent stem cells". Biochemical and Biophysical Research Commun. 474 (1): 91-96 (2016).
4. Nishimura K. et al., "Estradial facilitates functional integration of iPSC-derived dopaminergic neurons into striatal neuronal circuits via activation of integrin a5b1". Stem Cell Reports 6 (4): 511-524 (2016).
5. Matsuno K. et al., "Redefining definitive endoderm subtypes by robust induction of human induced pluripotent stemcells". Differentiation 2016.04.002.
6. Hayashi R. et al., "Co-ordinated ocular development ofrom human iPS cells and recovery of corneal function". Nature 531, 368-80 (2016),
7. Sasaki K. et al., "Robust in vitro induction of human germ celll fate from pluripotent stem cells". Cell Stem Cell 17 (2):178-194 (2015).
8. Okumura N. et al., "Laminin-511 and -521 enable efficient in vitro expansion of human corneal endothelial cells". Invest Ophthalmal Vis Sci. 56 (5), 2933-42 (2015).
9. Nakagawa M. et al., "A novel efficient feeder-free culture system for the derivation of human induced pluripotent stem cells". Scientific Reports 4: 3594 (2014).
10. Miyazaki T. et al. "Laminin E8 fragments support efficient adhesion and expansion of dissociated human pluripotentn stem cells. Nature Communications 3: 1236 (2012).
11. Taniguchi Y. et al., "The C-terminal region of laminin β-chains modulates the integrin-binding affinities of laminins:" J. Biol. Chem. 284 (12): 7820-31 (2009).
12. Ido H. et al., "The requirement of the glutamic acid residue at the third position from the carboxyl termini of the laminin gamma-chains in integrin-binding by lamiinins. J. Biol. Chem. 282 (15): 11144-54 (2017).