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
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.
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 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.
Citations 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.
Citations: Showing 1 - 2
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Extracellular matrix protein-1 secretory isoform promotes ovarian cancer through increasing alternative mRNA splicing and stemness
Authors: H Yin, J Wang, H Li, Y Yu, X Wang, L Lu, C Lv, B Chang, W Jin, W Guo, C Ren, G Yang
Nature Communications, 2021;12(1):4230.
Sample Types: Whole Cells
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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