Recombinant Human ECM1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human ECM1 Protein, CF Summary

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.

Applications/Dilutions

Dilutions
  • Bioactivity
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
Read Publications using
3937-EC in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human ECM1 Protein, CF

  • ECM1
  • extracellular matrix protein 1
  • p85
  • Secretory Component Glycoprotein
  • Secretory Component P85

Background

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).

  1. Chan, I. (2004) Exp. Dermatol. 29:52.
  2. Smits, P. et al. (1997) Genomics 45:487.
  3. Bhalerao, J. et al. (1995) J. Biol. Chem 270:16385.
  4. Smits, P. et al. (2000) J. Invest. Dermatol. 114:718.
  5. Mongiat, M. et al. (2003) J. Biol. Chem. 278:17491.
  6. Han, Z. et al. (2001) FASEB J. 15:988.
  7. Wang, L. et al. (2003) Cancer Lett. 200:57.
  8. Hamada, T. et al. (2003) J. Invest. Dermatol. 120:345.
  9. Oyama, N. et al. (2004) J. Clin. Invest. 113:1550.
  10. Fujimoto, N. et al. (2005) Biochem. Biophys. Res. Commun. 333:1327.

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Bioinformatics

Gene Symbol ECM1
Uniprot