{"title":"Cathepsin","description":"\u003ch3 class=\"highlited\" data-mce-fragment=\"1\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eAbout Cathepsin:\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp data-mce-fragment=\"1\"\u003eCathepsin is an enzyme known as a protease that’s found in all animals.\u003cbr data-mce-fragment=\"1\"\u003eThey are found in all animals due to the fact that they are essential to the mammalian cellular turnover process. In layman’s terms, cathepsins help to break down polypeptides, also known as amino acids or peptide bonds, to free the protein. Without this degradation, it wouldn’t absorb into the bloodstream and there would be no benefits to consuming it in the first place.\u003cbr data-mce-fragment=\"1\"\u003eThere are three primary forms of protease – serine, cysteine and aspartyl. Within these categories, there are subsections of cathepsins that range from A through to Z.\u003cbr data-mce-fragment=\"1\"\u003eCathepsin deficiencies are linked to a variety of illnesses and diseases, from cancer to strokes and Alzheimer’s. There is even evidence to suggest it can lead to macular degradation as well as pancreatitis.\u003c\/p\u003e\n\u003cp data-mce-fragment=\"1\"\u003e\u003cstrong data-mce-fragment=\"1\"\u003eCathepsin Function\u003c\/strong\u003e\u003cbr data-mce-fragment=\"1\"\u003eThe activity tales place almost entirely in the lysosome organelles as they are usually found in lysosomes. They hold enzymes that were formed in the cell and use them for digesting the peptide bonds in the cathepsin protein. Lysosomes can break various biomolecules, which might be why cathepsins are found there. However, there is one cathepsin that doesn’t adhere to this process. Cathepsin K works extracellularly after osteoclast secretion in bone resorption. The process is a type of cellular turnover that happens outside of the cell, unlike the other forms of cathepsin.\u003c\/p\u003e\n\u003cp data-mce-fragment=\"1\"\u003e\u003cstrong data-mce-fragment=\"1\"\u003eCathepsin Mechanism and Structure\u003c\/strong\u003e\u003cbr data-mce-fragment=\"1\"\u003eCathepsins are activated at low pH levels and they won’t work if the blood is too alkaline. They prefer acidity, and it can be an issue because normal blood sugar levels are neutral, bordering on alkaline. Most people register a 7.4pH level and alkalosis is a pH level of 7.45 or higher, so the degradation might not be automatic.\u003cbr data-mce-fragment=\"1\"\u003eEating sugary foods can help with the absorption of cathepsins in the blood, as can ingesting starchy foods such as complex carbs.Cathepsin is identified through a process called zymography. By separating them, loading them into a gel and leaving them overnight, the cathepsins break down the gel. Once this happens, they can be identified based on the migration distances and weights.\u003c\/p\u003e","products":[{"product_id":"ctsa-mouse","title":"CTSA Mouse","description":"\u003cp\u003eCathepsin-A Mouse Recombinant\u003c\/p\u003e\n\n\u003cdiv class=\"synonyms_hide\"\u003e\n  \u003cp\u003eLysosomal\nprotective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin\nA, Protective protein cathepsin A, PPCA, Protective protein 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