Recombinant Human Laminin alpha 4 Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Citations (5)
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Recombinant Human Laminin alpha 4 Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by the ability of the immobilized protein to support the adhesion of HT1080 human fibrosarcoma cells. The ED50 for this effect is 0.7-2.8 μg/mL.
Optimal dilutions should be determined by each laboratory for each application.
Chinese Hamster Ovary cell line, CHO-derived human Laminin alpha 4 protein
Gln826-Ala1816, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gln826 predicted, sequencing might be blocked, no result obtained
Structure / Form
Predicted Molecular Mass
111 kDa
110-120 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 200 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Laminin alpha 4

The alpha 4 chain of laminin (LAMA4) is a secreted ~210 kDa glycoprotein that contributes to the formation of LN411 (laminin-8, subunits alpha 4 beta 1 gamma 1), LN421 (laminin-9, subunits alpha 4 beta 2 gamma 1), and LN423 (laminin-14, subunits alpha 4 beta 2 gamma 3) (1-4). Laminin alpha,  beta  and  gamma  subunits interact via alpha -helical domains to create cruciform, disulfide-linked, coiled-coil laminin heterotrimers (1, 2). LAMA4 is mainly expressed in mesodermal tissues, and is produced by endothelium, cardiac and skeletal muscle fibers, lung mesenchymal cells, pre-adipocytes, kidney mesangial cells, peripheral nerves and neutrophils (3-8). It is found in the subendothelium in muscle, brain, and bone marrow, and in heart, skin, and the perineurium of peripheral nerves (3-7, 9, 10). The human LAMA4 cDNA encodes 1823 amino acids (aa), including a 24 aa signal sequence and a 1799 aa mature protein that contains three EGF-like repeats (aa 82-240) followed by five coiled-coil regions (aa 320-806) and five globular, laminin G-like (LG) domains (aa 833-1820). Potential isoforms of 1816 aa and 1791 aa are lacking sequences following the EGF-like repeats. A protease-sensitive region between LG3 and LG4 produces a processed ~180 kDa form that is detected in vivo (9, 10). Within the LG region, human and mouse LAMA4 share 91% aa sequence identity. LAMA4 LG domains serve as Ca++-mediated receptors for integrins such as alpha v beta 3 and alpha 3 beta 1 (mainly at LG2), fibulin-1 and -2 (multiple LG), and heparan sulfate proteoglycans such as syndecans 2 and 4 (mainly at LG4) (8-12). Deletion of LAMA4 in mice results in misalignment of pre- and post-synaptic membranes at neuromuscular junctions, faulty nerve myelination, chronic kidney disease, deficient neutrophil extravasation, and microvessel instability, which causes cardiomyopathy and circulatory dysfunctions (5-8, 12-14). These results show the importance of LAMA4-containing laminins in normal synapse maturation and blood vessel maturation.

  1. Tzu, J. and M.P. Marinkovich (2008) Int. J. Biochem. Cell Biol. 40:199.
  2. Durbeej, M. (2010) Cell Tiss. Res. 339:259.
  3. Liu, J. et al. (1996) Matrix Biol. 15:433.
  4. Iivanainen, A. et al. (1997) J. Biol. Chem. 272:27862.
  5. Patton, B.L. et al. (2001) Nat. Neurosci. 4:597.
  6. Wallquist, W. et al. (2005) J. Neurosci. 25:3692.
  7. Abrass, C.K. et al. (2010) Am. J. Pathol. 176:839.
  8. Wondimu, Z. et al. (2004) Blood 104:1859.
  9. Matsuura, H. et al. (2004) J. Invest. Dermatol. 122:614.
  10. Talts, J.F. et al. (2000) J. Biol. Chem. 275:35192.
  11. Gonzalez, A.M. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16075.
  12. DeHahn, K.C. et al. (2004) Exp. Cell Res. 294:281.
  13. Thyboll, J. et al. (2002) Mol. Cell Biol. 22:1194.
  14. Wang, J. et al. (2006) J. Biol. Chem. 281:213.
Entrez Gene IDs
3910 (Human); 16775 (Mouse); 309816 (Rat)
Alternate Names
DKFZp686D23145; LAMA3LAMA4*-1; LAMA4; laminin alpha 4 chain; Laminin alpha 4; laminin subunit alpha-4; laminin, alpha 4; Laminin-14 subunit alpha; Laminin-8 subunit alpha; Laminin-9 subunit alpha

Citations for Recombinant Human Laminin alpha 4 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

5 Citations: Showing 1 - 5
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  1. Integrins and extracellular matrix proteins modulate adipocyte thermogenic capacity
    Authors: MA Gonzalez P, K Stojkova, MK Vaicik, A Pelowe, A Goddi, A Carmona, B Long, AA Qutub, A Gonzalez, RN Cohen, EM Brey
    Scientific Reports, 2021;11(1):5442.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. LAMA4 upregulation is associated with high liver metastasis potential and poor survival outcome of Pancreatic Cancer
    Authors: B Zheng, J Qu, K Ohuchida, H Feng, SJF Chong, Z Yan, Y Piao, P Liu, N Sheng, D Eguchi, T Ohtsuka, K Mizumoto, Z Liu, S Pervaiz, P Gong, M Nakamura
    Theranostics, 2020;10(22):10274-10289.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Pathological Progression Induced by the Frontotemporal Dementia-Associated R406W Tau Mutation in Patient-Derived iPSCs
    Authors: M Nakamura, S Shiozawa, D Tsuboi, M Amano, H Watanabe, S Maeda, T Kimura, S Yoshimatsu, F Kisa, CM Karch, T Miyasaka, A Takashima, N Sahara, SI Hisanaga, T Ikeuchi, K Kaibuchi, H Okano
    Stem Cell Reports, 2019;13(4):684-699.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  4. Direct contact with perivascular tumor cells enhances integrin �v?3 signaling and migration of endothelial cells
    Authors: ME Burgett, JD Lathia, P Roth, AS Nowacki, DS Galileo, E Pugacheva, P Huang, A Vasanji, M Li, T Byzova, T Mikkelsen, S Bao, JN Rich, M Weller, CL Gladson
    Oncotarget, 2016;7(28):43852-43867.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Monoclonal antibodies to human laminin alpha4 chain globular domain inhibit tumor cell adhesion and migration on laminins 411 and 421, and binding of alpha6beta1 integrin and MCAM to alpha4-laminins.
    Authors: Ishikawa T, Wondimu Z, Oikawa Y, Ingerpuu S, Virtanen I, Patarroyo M
    Matrix Biol, 2014;36(0):5-14.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay


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