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ST7/LRP12: cDNA Clones

ST7 (Suppressor of Tumorigenicity 7), also known as RAY1, TSG7 and FAM4A1, is a type I transmembrane protein belonging to the LDLR superfamily and is designated LRP12. Human ST7 shares 95% aa sequence homology with mouse and rat, 96% with canine, and 98% with bovine, equine and porcine ST7 within the ECD. Genomic sequencing indicates the possibility of up to 18 splicing isoforms, but expression of these has not been well studied. ST7 is widely expressed in normal tissues, especially fibroblasts. Highest mRNA levels were detected in heart and skeletal muscle. ST7 was originally proposed to be a tumor suppressor protein, but it is not consistently downregulated in a variety of cancers, either by mutation or loss of heterozygosity. In certain cancers, expression may even be upregulated. Expression may be associated with downregulated expression of extracellular matrix molecules that are involved in remodeling, such as SPARC, IGFBP-5 and several matrix metalloproteinases, and modulation of in vivo tumorigenicity.

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2 results for "ST7/LRP12 cDNA Clones" in Products

ST7/LRP12: cDNA Clones

ST7 (Suppressor of Tumorigenicity 7), also known as RAY1, TSG7 and FAM4A1, is a type I transmembrane protein belonging to the LDLR superfamily and is designated LRP12. Human ST7 shares 95% aa sequence homology with mouse and rat, 96% with canine, and 98% with bovine, equine and porcine ST7 within the ECD. Genomic sequencing indicates the possibility of up to 18 splicing isoforms, but expression of these has not been well studied. ST7 is widely expressed in normal tissues, especially fibroblasts. Highest mRNA levels were detected in heart and skeletal muscle. ST7 was originally proposed to be a tumor suppressor protein, but it is not consistently downregulated in a variety of cancers, either by mutation or loss of heterozygosity. In certain cancers, expression may even be upregulated. Expression may be associated with downregulated expression of extracellular matrix molecules that are involved in remodeling, such as SPARC, IGFBP-5 and several matrix metalloproteinases, and modulation of in vivo tumorigenicity.

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