Matrixome iMatrix 221 Cardiac and Myoblast Cell Culture Substrate

Code: NP892-06
  • $684.00
  • (Delivery from $80.00 )
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Recombinant Laminin-221 E-8 Fragments

iMatrix-221's 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-221

iMatrix-221 is a highly purified and refined product of human recombinant laminin-221 (E8 fragment) expressed by CHO-S cells. Laminin-221 is found predominantly in the basal lamina of striated muscle tissues. Expression deficiencies are implicated in muscular dystophy and cardiomyopathies.1

Laminins of the α-2 type are also a predomiant form found in the human adult heart tissue.2 Cultivation of iPSC-drived cardiomyocytes on iMatrix-221 has been demonstrated to maintain strong contractility in attached monolayer culture.3

Product Name

iMatrix-221 Cardiac and Myoblast Cell Culture Substrate

Catalog Number




  • NP892-061 — 2 × 175 µg
  • NP892-062 — 6 × 175 µg

Molecular Weight

150 kDa


>95% pure


Purified Laminin-221 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: Kd for integrin binding



Notice To Purchaser

REPROCELL is a licensed distributor of Matrixome cell culture substrates to the global market.

Recommended Usage

iMatrix-221 is suitable for use as a substrate for culture of various myoblast cell types, but most notably for cardiomyocytes.


500 µg/mL


CHO-S cell expression


Matrixome Corporation (Japan)

  1. Oliviero P., Expression of laminin α2 chain during normal and pathological growth of myocardium in rat and human. Cardiovascular Research 46, 346-355 (2000).
  2. Ja K.P. Myu Mia, PSC-derived human cardiac progenitor cells improve ventricular remodeling via angiogenesis and interstitial networking of infarcted myocardium. J Cell Mol Med 20(2), 323-332 (2016).
  3. unpublished, Osaka University(2018).
  4. Miyazaki T. et al. Laminin E8 fragments support efficient adhesion and expansion of dissociated human pluripotent stem cells. Nature Communications 3: 1236 (2012).
  5. 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).
  6. 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 laminins. J. Biol. Chem. 282 (15): 11144-54 (2017).