Western blot analysis of Cystatin C was performed following immunoprecipitation of Cystatin C-FLAG with an anti-FLAG antibody from ARPE-19 cells transfected with a construct encoding a FLAG-tagged Cystatin C. Following immunoprecipitation, proteins were transferred to a nitrocellulose membrane, blocked, and then probed with a Cystatin C polyclonal antibody (Product # PA5-19108) at a dilution of 1:500 for 1 hour at room temperature. The blot was washed, and probed with a DyLight 800-conjugated anti-goat IgG secondary antibody at a dilution of 1:10,000 for 40 minutes at room temperature. Detection was performed using a near IR imager. Data courtesy of the Innovators Program.
|Tested species reactivity||Human|
|Host / Isotype||Goat / IgG|
|Immunogen||Synthetic peptide sequence (SVEEEGVRRALD) corresponding to the internal amino acids of CST3|
|Purification||Antigen affinity chromatography|
|Storage buffer||TBS, pH 7.3, with 0.5% BSA|
|Contains||0.02% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||0.3-1 ug/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins , type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease.
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