Human Laminin 332

Human Laminin 332

This human laminin 332 protein was purified from the conditioned medium of immortalized 184A1 mammary epithelial cells via affinity and size-exclusion chromatography.

Laminin 332 (formerly laminin 5) is a heterotrimeric basement membrane protein composed of the alpha3, beta3 and gamma2 chains of laminin. It is expressed in skin, breast and other tissues, where it is involved in formation of hemidesmosomes and wound healing. Laminin 332 has been implicated in cancer progression. In breast cancer, laminin 332 has been identified as a microenvironmental protein which can act as a motility factor.

From the laboratory of Philip M. Carpenter, MD, University of Southern California.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EUV102
Human Laminin 332, 100ug
100ug Currently unavailable
Regular Price:$1,185.00
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Specifications

Product Type: Protein
Name: Human Laminin 332 (Alternative names: laminin 5,laminin V, epiligrin, kalinin, ladsin, nicein).
Accession ID: Q16787, NP_937762.1, Q13751, NP_000219.2, Q13753, NM_005562
Source: 184A1 human mammary epithelial cell conditioned media
Molecular Weight: 450 kDa, unprocessed
Amino Acid Sequence: Sequences available upon request.
Fusion Tag(s): None
Purity: Approximately 90%, Assessed by SDS PAGE.
Buffer: 150 mM NaCl, 10 mM Tris, pH 7.4, filter sterile
Stability: Stable when kept at -20C (or lower), at the concentration provided. IMPORTANT: Rapidly lose in ability to provide cell detachment when stored after being diluted. It is suggested to thaw once into aliquots prior to dilution and diluting the aliquots immediately as needed for experiments. Aliquots should be stored in sterile polycarbonate ependorff tubes.
Concentration: See product packaging. Concentration determined by OD280 of a standard curve of Bovine Seum Albumin (Concentration ≈ OD280 x 1.788)
Comments: Filter Sterile, both processed and unprocessed forms are present.
Storage: -20C or lower (Thawed protein retains activity for 1 month if stored at 4 C).
Shipped: Dry ice

Data

Motility and invasion by purified laminin 332

Laminin 332 Figure

A scattering assay done using purified laminin 332 (designated laminin 5 in the figure) showed dose-dependent motility.

Adapted from: Carpenter PM, Dao AV, Arain ZS, et al. Motility induction in breast carcinoma by mammary epithelial laminin 332 (laminin 5). Mol Cancer Res. 2009;7(4):462-75.

Provider
From the laboratory of Philip M. Carpenter, MD, University of Southern California.
Comments

Scattering Assay: 10 ug/mL will induce scattering of 50% of MCF-7 cells after 24 hour incubation. For more details/methods on the scattering assay see: Carpenter PM, Dao AV, Arain ZS, et al. Motility induction in breast carcinoma by mammary epithelial laminin 332 (laminin 5). Mol Cancer Res. 2009;7(4):462-75.

Coating Dishes/Plates: The protein storage buffer (150 mM NaCl, 10 mM Tris, pH 7.4) will work fine, as well as PBS, hepes, or RPMI. It is suggested to start at 10 ug/ml or 100 ng in 100ul of buffer for a 96 well plate, and optimize from there. Allow 4 hours for coating, but overnight is better.

References
  1. Aumailley M, Bruckner-Tuderman L, Carter WG, et al. A simplified laminin nomenclature. Matrix Biol. 2005;24(5):326-332.
  2. Goldfinger LE, Hopkinson SB, deHart GW, Collawn S, Couchman JR, Jones JC. The alpha-3 laminin subunit, alpha-6-beta-4 and alpha-3-beta-1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J Cell Sci. 1999;112(Pt 16):2615-2629.
  3. Patarroyo M, Tryggvason K, Virtanen I. Laminin isoforms in tumor invasion, angiogenesis and metastasis. Semin Cancer Biol 2002;12(3):197-207
  4. Carpenter PM, Dao AV, Arain ZS, et al. Motility induction in breast carcinoma by mammary epithelial laminin 332 (laminin 5). Mol Cancer Res. 2009;7(4):462-75.
  5. Guess CM, Quaranta V. Defining the role of laminin-332 in carcinoma. Matrix Biol. 2009;28(8):445-55.
  6. Carpenter PM, Sivadas P, Hua SS, Xiao C, Gutierrez AB, Ngo T, Gershon PD. Migration of breast cancer cell lines in response to pulmonary laminin 332. Cancer Med. 2016 Nov 22. doi: 10.1002/cam4.957. View Article
  7. Muranen T, Iwanicki MP, Curry NL, Hwang J, DuBois CD, Coloff JL, Hitchcock DS, Clish CB, Brugge JS, Kalaany NY. Starved epithelial cells uptake extracellular matrix for survival. Nat Commun. 2017 Jan 10;8:13989. Cell Rep. 2017 Jan 10;18(2):334-343. View Article
  8. Wang H, Jin H, Beauvais DM, Rapraeger AC. Cytoplasmic domain interactions of syndecan-1 and syndecan-4 with α6β4 integrin mediate human epidermal growth factor receptor (HER1 and HER2)-dependent motility and survival. J Biol Chem. 2014 Oct 31;289(44):30318-32. doi: 10.1074/jbc.M114.586438. PubMed PMID: 25202019; PubMed Central PMCID: PMC4215216. View Article
  9. Carpenter PM, Ziogas A, Markham EM, Cantillep AS, Yan R, Anton-Culver H. Laminin 332 expression and prognosis in breast Cancer. Hum Pathol. 2018 Aug 17. pii: S0046-8177(18)30307-1. View Article
  10. Chen M, Choi S, Jung O, Wen T, Baum C, Thapa N, Lambert PF, Rapraeger AC, Anderson RA. The Specificity of EGF-Stimulated IQGAP1 Scaffold Towards the PI3K-Akt Pathway is Defined by the IQ3 motif. Sci Rep. 2019 Jun 24;9(1):9126. View Article
  11. Fouillen A, Grenier D, Barbeau J, Baron C, Moffatt P, Nanci A. Selective bacterial degradation of the extracellular matrix attaching the gingiva to the tooth. Eur J Oral Sci. 2019 Aug;127(4):313-322. View Article
  12. Nakhaei K, Ishijima M, Ikeda T, Ghassemi A, Saruta J, Ogawa T. Ultraviolet Light Treatment of Titanium Enhances Attachment, Adhesion, and Retention of Human Oral Epithelial Cells via Decarbonization. Materials (Basel). 2020 Dec 31;14(1):151. View article

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