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  2. Cathepsin - Wikipedia

    en.wikipedia.org/wiki/Cathepsin

    This cathepsin zymography protocol has been used to detect femtomole quantities of mature cathepsin K. [23] The different cathepsins can be identified based on their migration distance due to their molecular weights: cathepsin K (~37 kDa), V (~35 kDa), S (~25kDa), and L (~20 kDa). Cathepsins have specific pH levels at which they have optimum ...

  3. Cathepsin L1 - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_L1

    Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. [ 3 ] [ 4 ] [ 5 ] The protein is a cysteine cathepsin , a lysosomal cysteine protease that plays a major role in intracellular protein catabolism .

  4. Cathepsin L - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_L

    Cathepsin L may refer to: Cathepsin L1 , a human protease enzyme encoded by the CTSL gene and known for its role in viral entry Cathepsin L2 , a human protease enzyme encoded by the CTSV gene and also known as cathepsin V

  5. Keratinocyte - Wikipedia

    en.wikipedia.org/wiki/Keratinocyte

    The primary function of keratinocytes is the formation of a barrier against environmental damage by heat, UV radiation, dehydration, pathogenic bacteria, fungi, parasites, and viruses.

  6. Cathepsin L2 - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_L2

    1515 13039 Ensembl ENSG00000136943 ENSMUSG00000021477 UniProt O60911 P06797 RefSeq (mRNA) NM_001333 NM_001201575 NM_009984 RefSeq (protein) NP_001188504 NP_001324 NP_034114 Location (UCSC) Chr 9: 97.03 – 97.16 Mb Chr 13: 64.51 – 64.52 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in ...

  7. Cysteine protease - Wikipedia

    en.wikipedia.org/wiki/Cysteine_protease

    The activity of cysteine proteases is regulated by a few general mechanisms, which includes the production of zymogens, selective expression, pH modification, cellular compartmentalization, and regulation of their enzymatic activity by endogenous inhibitors, which seemingly is the most efficient mechanism associated with the regulation of the ...

  8. E-64 - Wikipedia

    en.wikipedia.org/wiki/E-64

    E-64 is an epoxide which can irreversibly inhibit a wide range of cysteine peptidases.. The compound was first isolated and identified from Aspergillus japonicus in 1978. [1] It has since been shown to inhibit many cysteine peptidases such as papain, cathepsin B, cathepsin L, calpain and staphopain.

  9. Calpain - Wikipedia

    en.wikipedia.org/wiki/Calpain

    A calpain (/ ˈ k æ l p eɪ n /; [1] EC 3.4.22.52, EC 3.4.22.53) is a protein belonging to the family of calcium-dependent, non-lysosomal cysteine proteases (proteolytic enzymes) expressed ubiquitously in mammals and many other organisms.

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