prospec

Cathepsin

  • Name
  • Description
  • Pricings
  • Quantity
  • CTSA Mouse
    More Info
  • Cathepsin-A Mouse Recombinant
  • Shipped with Ice Packs
  • CTSB Mouse
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  • Cathepsin-B Mouse Recombinant
  • Shipped with Ice Packs
  • CTSB Mouse, Active
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  • Cathepsin-B Mouse Recombinant, Active
  • Shipped with Ice Packs
  • CTSD Human
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  • Cathepsin-D Human Recombinant
  • Shipped with Ice Packs
  • CTSD Mouse
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  • Cathepsin-D Mouse Recombinant
  • Shipped with Ice Packs
  • CTSE Human
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  • Cathepsin-E Human Recombinant
  • Shipped with Ice Packs
  • CTSF Human
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  • Cathepsin-F Human Recombinant
  • Shipped with Ice Packs
  • CTSL Human
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  • Cathepsin-L Human Recombinant
  • Shipped with Ice Packs
  • CTSL Mouse
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  • Cathepsin-L Mouse Recombinant
  • Shipped with Ice Packs
  • CTSS Human
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  • Cathepsin-S Human Recombinant
  • Shipped with Ice Packs
  • CTSS Mouse
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  • Cathepsin-S Mouse Recombinant
  • Shipped with Ice Packs
  • CTSW Human
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  • Cathepsin-W Human Recombinant
  • Shipped with Ice Packs
  • CTSZ Human
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  • Cathepsin-Z Human Recombinant
  • Shipped with Ice Packs
  • CTSZ Human, Sf9
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  • Cathepsin-Z Human Recombinant, Sf9
  • Shipped with Ice Packs
  • CTSZ Mouse
    More Info
  • Cathepsin-Z Mouse Recombinant
  • Shipped with Ice Packs

About Cathepsin:

Cathepsin is an enzyme known as a protease that’s found in all animals.
They 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.
There 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.
Cathepsin 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.

Cathepsin Function
The 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.

Cathepsin Mechanism and Structure
Cathepsins 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.
Eating 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.