Recombinant Mouse ST7/LRP12 Protein, CF Summary
Product Specifications
Glu33-Thr491, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
7910-S7
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 200 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: ST7/LRP12
ST7 (Suppressor of Tumorigenicity 7), also known as RAY1, TSG7 and FAM4A1, is a type I transmembrane protein belonging to the LDLR (low density lipoprotein receptor) superfamily and is designated LRP12 (1‑3). The mouse ST7 cDNA encodes 858 amino acids (aa) including a 32 aa signal sequence, a 460 aa extracellular domain (ECD) containing two CUB domains and five LDLR class A domains, a 21 aa transmembrane domain, and a 345 aa cytoplasmic domain containing motifs implicated in endocytosis and signal transduction (1, 2). Mouse ST7 shares 97% aa sequence homology rat, and 95% with human, bovine, equine and porcine ST7 within the ECD. A mouse ST7 splicing variant lacks aa 27‑45, and another potential variant has an alternate start site at aa 188. ST7 is widely expressed in normal tissues, especially on fibroblasts (1, 4). Highest mRNA levels are detected in heart and skeletal muscle (1). ST7 was originally proposed to be a tumor suppressor protein, but it is not consistently down‑regulated in a variety of cancers, either by mutation or loss of heterozygosity (1, 4‑7). In certain cancers, expression may even be up‑regulated (8). Expression may be associated with down‑regulated expression of extracellular matrix molecules that are involved in remodeling, such as SPARC, IGFBP5 and several matrix metalloproteinases, and modulation of in vivo tumorigenicity (4, 5).
- Qing, J. et al. (1999) Oncogene 18:335.
- Battle, M.A. et al. (2003) Biochemistry 42:7270.
- Vincent, J.B. et al. (2002) Genomics 80:283.
- Zenclusen, J.C. et al. (2001) Nat. Genet. 27:392.
- Hooi, C.F. et al. (2006) Oncogene 25:3924.
- Sivasundaram, K. et al. (2003) Oncol. Rep. 10:1737.
- Dong, S.M. and D. Sidransky (2002) Clin. Cancer Res. 8:2939.
- Garnis, C. et al. (2004) Oncogene 23:2582.
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