Measured by the ability of the immobilized protein to support the adhesion of A431 human epithelial carcinoma cells.
When 5 x 10 4 cells/well are added to rhSMOC-1 coated plates, cell adhesion is enhanced in a dose dependent manner after 75 minutes at 37 degreesC. The ED 50 for this effect is 0.5-2 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human SMOC-1 protein His27-Val434, with a C-terminal 6-His tag
>95%, 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
46.1 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
60-65 kDa, reducing conditions
Publications
Read Publication using 6074-SM in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human SMOC-1 Protein, CF
Secreted modular calcium-binding protein 1
SMOC1
SMOC-1
SPARC related modular calcium binding 1
SPARC-related modular calcium-binding protein 1
Background
SMOC-1 (secreted, or SPARC-related, modular calcium-binding protein 1) is a 70 - 90 kDa secreted glycoprotein that is a member of the SPARC family of matricellular molecules (1). Mature human SMOC-1 is 408 amino acids (aa) in length. It contains one Kazal-like domain (aa 42 - 87), two thyroglobulin type-1 (TY) segments (aa 92 - 159 and 224 - 292) and two EF-hand sequences (aa 359 - 394 and 396 - 431). One potential splice variant contains a 16 aa region of alternate sequence between the TY domains, a 7 aa deletion between the TY and EF-hand domains, and three alternate aa at the C-terminus. Mature human SMOC-1 shares 92% aa identity with mouse and rat SMOC-1 and 97%, 96% and 95% aa identity with canine, bovine and porcine SMOC-1, respectively. The principal difference between rodents and other mammals is an additional 19 aa near the C-terminus of rodent SMOC-1. Like other matricellular proteins, SMOC-1 is primarily expressed in basement membranes, although it has also been found in other extracellular matrices and the oocyte zona pellucida (1). It is present early in mouse embryogenesis, and is produced by cells deriving from all three germ layers (4). Recombinant bacterially produced human SMOC-1 and SMOC-2 were both shown to bind the acute phase protein, C-reactive protein, and the adhesion proteins, fibulin and vitronectin (2). A signaling role for SMOC-1 was shown in rat mesangial cells: induction of nitric oxide in response to inflammatory cytokines downregulates SMOC-1 which, in turn, downregulates expression of TGF-beta and TGF-beta -regulated genes. This mechanism is proposed to limit the profibrotic effects of TGF-beta , for example in the glomerulus (5). In Xenopus, the SMOC paralog has been shown to antagonize BMP activity.
Vannahme, C. et al. (2002) J. Biol. Chem. 277:37977.
Novinec, M. et al. (2008) Protein Expr. Purif. 62:75.
Entrez Q8BLY1 and EDL02699.
Gersdorff, N. et al. (2006) Histochem. Cell Biol. 126:705.
Dreieicher, E. et al. (2009) J. Am. Soc. Nephrol. 20:1963.
Thomas, J.T. et al. (2009) J. Biol. Chem. 284:18994.
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