Human ECM-1 Antibody Summary
Accession # Q16610
This antibody functions as an ELISA capture antibody when paired with Mouse Anti-Human ECM‑1 Monoclonal Antibody (Catalog # MAB3937).
This product is intended for assay development on various assayplatforms requiring antibody pairs.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human ECM‑1 by Western Blot. Western blot shows lysates of CCD‑1070Sk human foreskin fibroblast cell line and WS‑1 human fetal skin fibroblast cell line. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human ECM‑1 Monoclonal Antibody (Catalog # MAB39371) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for ECM‑1 at approximately 75 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 3.
Human ECM‑1 ELISA Standard Curve. Recombinant human ECM-1 protein was serially diluted 2-fold and captured by Mouse Anti-Human ECM-1 Monoclonal Antibody (Catalog # MAB39371) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human ECM-1 Monoclonal Antibody (Catalog # MAB3937) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
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