Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of B16‑F1 mouse melanoma cells. When 5 x 104 cells/well are added to Recombinant Human ECM-1 coated plates (10 µg/mL with 100 µL/well), >30% will adhere after 30 minutes at 37 °C. Optimal concentration depends on cell type as well as the application or research objective. |
Source | Mouse myeloma cell line, NS0-derived human ECM1 protein Ala20-Glu540, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Ala20 |
Protein/Peptide Type | Recombinant Proteins |
Gene | ECM1 |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
|
|
Theoretical MW | 59.7 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
|
SDS-PAGE | 77-87 kDa, reducing conditions |
|
Publications |
|
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
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).
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.