Recombinant Human ECM1 Protein, CF
Recombinant Human ECM1 Protein, CF Summary
Optimal concentration depends on cell type as well as the application or research objective.
Ala20-Glu540, with a C-terminal 6-His tag
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile 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.
Extracellular matrix protein-1 (ECM-1) is an 85 kDa, secreted glycoprotein important in connective tissue organization (1-3). Of three identified splice variants the 540 amino acid (aa) form, ECM-1a, is the most widely expressed, with the highest expression in the placenta and heart (2). ECM-1b (415 aa) is found only in tonsil and associated with suprabasal keratinocytes (2, 4). Since ECM-1b expression is differentiation-dependent, a role in terminal keratinocyte differentiation has been suggested (4). ECM-1c (559 aa) accounts for approximately 15% of skin ECM-1 (5). Human ECM-1a contains a 19 aa signal peptide and a 521 aa secreted portion that includes an N-terminal proline-rich, cysteine-free region, two tandem repeat domains, and a C-terminal domain. There are six repeats of a CC(X7-10)C motif
(x = any aa) within the tandem repeat and C-terminal domains. These motifs are involved in ligand binding to members of the albumin family, and are expected to form two (in ECM-1b) or three (in ECM-1a) “double loop” structures (2). Mature human ECM-1a shows 69%, 71%, 72% and 76% aa identity with corresponding isoforms of mouse, rat, canine, and bovine ECM-1, respectively. ECM-1 is over-expressed in many malignant epithelial tumors and has demonstrated angiogenic activity (6, 7). A variety of ECM-1 mutations, mainly within the first tandem repeat, are considered causative of lipoid proteinosis, a condition showing thickened and irregular extracellular matrix within connective tissue (8). In the autoimmune condition lichen sclerosis, auto-antibodies mainly recognize the second tandem repeat or the
C-terminus of ECM-1 (9). These domains also bind the extracellular matrix molecules fibulin-1 and perlecan (5, 10). The phenotypes of lipoid proteinosis and lichen sclerosis support a role for ECM-1 as a “biological glue” in the dermis (1).
- Chan, I. (2004) Exp. Dermatol. 29:52.
- Smits, P. et al. (1997) Genomics 45:487.
- Bhalerao, J. et al. (1995) J. Biol. Chem 270:16385.
- Smits, P. et al. (2000) J. Invest. Dermatol. 114:718.
- Mongiat, M. et al. (2003) J. Biol. Chem. 278:17491.
- Han, Z. et al. (2001) FASEB J. 15:988.
- Wang, L. et al. (2003) Cancer Lett. 200:57.
- Hamada, T. et al. (2003) J. Invest. Dermatol. 120:345.
- Oyama, N. et al. (2004) J. Clin. Invest. 113:1550.
- Fujimoto, N. et al. (2005) Biochem. Biophys. Res. Commun. 333:1327.
Citation for Recombinant Human ECM1 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.
1 Citation: Showing 1 - 1
Protective effect of stromal Dickkopf-3 in prostate cancer: opposing roles for TGFBI and ECM-1
Authors: Z Al Shareef, H Kardooni, V Murillo-Ga, G Domenici, E Stylianaki, JH Steel, M Rabano, I Gorroño-Et, I Zabalza, M dM Vivanco, J Waxman, RM Kypta
Sample Types: Whole Cells
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