Mouse/Rat SMOC-1 Antibody
Mouse/Rat SMOC-1 Antibody Summary
Accession # AAD41590
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 Mouse and Rat SMOC‑1 Isoform 2 by Western Blot. Western blot shows lysates of rat ovary tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse/Rat SMOC-1 Isoform 2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5550) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for SMOC-1 Isoform 2 at approximately 70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.
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.
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 mouse SMOC-1 is 427 amino acids (aa) in length. It contains one Kazal-like domain (aa 42‑86), two thyroglobulin type-1 segments (aa 91‑157 and 223‑291) and two functional EF-hand sequences (aa 358‑393 and 395‑430) (1, 2). Two splice variants contain an insertion of eleven aa after Lys174, with one of these also including an alternate start site at Met65 (3). Mature mouse SMOC-1 shares 99% aa identity with rat SMOC-1 and 92% aa identity with human, canine and bovine SMOC-1. 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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