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recombinant human catd  (Sino Biological)


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    Structured Review

    Sino Biological recombinant human catd
    Recombinant Human Catd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+catd/Human+Cathepsin+D+CTSD+Protein/pmc12707259-85-0-6
    Average 93 stars, based on 2 article reviews
    recombinant human catd - by Bioz Stars, 2026-10
    93/100 stars

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    Related Articles

    Recombinant:

    Article Title: Strategic Reduction of Hybrid Insulin Peptide Formation Significantly Delays Diabetes Onset in NOD Mice
    Article Snippet: .. Recombinant human CatD was obtained from Sino Biological (Houston, Texas, USA) and added to the mixtures at concentration of 0nM or 112.5nM. ..

    Concentration Assay:

    Article Title: Strategic Reduction of Hybrid Insulin Peptide Formation Significantly Delays Diabetes Onset in NOD Mice
    Article Snippet: .. Recombinant human CatD was obtained from Sino Biological (Houston, Texas, USA) and added to the mixtures at concentration of 0nM or 112.5nM. ..



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    recombinant human catd  (Sino Biological)
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    catd activity assay kit  (R&D Systems)
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    cathepsin d catd  (R&D Systems)
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    ( A ) Cleavage of VEGF-C by coincubation of pro-VEGF-C with <t>cathepsin</t> <t>D</t> (left panel) and secondary activation of ΔNΔC-VEGF-C (a mature form of VEGF-C translated from a truncated cDNA, right panel). ( B ) Quantification of the cleavage of pro-VEGF-C (n = 3) and ΔNΔC-VEGF-C (n = 2) by cathepsin D. ( C ) Cathepsin-D-mediated conversion of pro-VEGF-D into mature VEGF-D (left panel), and rapid activation of ΔNΔC-VEGF-D (a mature form of VEGF-D translated from a truncated cDNA, right panel). ( D ) Cleavage of pro-VEGF-D by KLK3. Note that, KLK3 cleaves VEGF-D between the VEGF homology domain and the N-terminal propeptide, but also between the VEGF homology domain and the C-terminal propeptide (for a detailed breakdown of the cleavage products visible in this overlay and the individual exposures, see ) (n = 2). 10.7554/eLife.44478.021 Figure 6—source data 1. Quantification of the cleavage of pro-VEGF-C and mature VEGF-C by cathepsin D.
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    recombinant human cathepsin d catd  (R&D Systems)
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    ( A ) Cleavage of VEGF-C by coincubation of pro-VEGF-C with <t>cathepsin</t> <t>D</t> (left panel) and secondary activation of ΔNΔC-VEGF-C (a mature form of VEGF-C translated from a truncated cDNA, right panel). ( B ) Quantification of the cleavage of pro-VEGF-C (n = 3) and ΔNΔC-VEGF-C (n = 2) by cathepsin D. ( C ) Cathepsin-D-mediated conversion of pro-VEGF-D into mature VEGF-D (left panel), and rapid activation of ΔNΔC-VEGF-D (a mature form of VEGF-D translated from a truncated cDNA, right panel). ( D ) Cleavage of pro-VEGF-D by KLK3. Note that, KLK3 cleaves VEGF-D between the VEGF homology domain and the N-terminal propeptide, but also between the VEGF homology domain and the C-terminal propeptide (for a detailed breakdown of the cleavage products visible in this overlay and the individual exposures, see ) (n = 2). 10.7554/eLife.44478.021 Figure 6—source data 1. Quantification of the cleavage of pro-VEGF-C and mature VEGF-C by cathepsin D.
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    human pro catd  (R&D Systems)
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    ( A ) Cleavage of VEGF-C by coincubation of pro-VEGF-C with <t>cathepsin</t> <t>D</t> (left panel) and secondary activation of ΔNΔC-VEGF-C (a mature form of VEGF-C translated from a truncated cDNA, right panel). ( B ) Quantification of the cleavage of pro-VEGF-C (n = 3) and ΔNΔC-VEGF-C (n = 2) by cathepsin D. ( C ) Cathepsin-D-mediated conversion of pro-VEGF-D into mature VEGF-D (left panel), and rapid activation of ΔNΔC-VEGF-D (a mature form of VEGF-D translated from a truncated cDNA, right panel). ( D ) Cleavage of pro-VEGF-D by KLK3. Note that, KLK3 cleaves VEGF-D between the VEGF homology domain and the N-terminal propeptide, but also between the VEGF homology domain and the C-terminal propeptide (for a detailed breakdown of the cleavage products visible in this overlay and the individual exposures, see ) (n = 2). 10.7554/eLife.44478.021 Figure 6—source data 1. Quantification of the cleavage of pro-VEGF-C and mature VEGF-C by cathepsin D.
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    Image Search Results


    ( A ) Cleavage of VEGF-C by coincubation of pro-VEGF-C with cathepsin D (left panel) and secondary activation of ΔNΔC-VEGF-C (a mature form of VEGF-C translated from a truncated cDNA, right panel). ( B ) Quantification of the cleavage of pro-VEGF-C (n = 3) and ΔNΔC-VEGF-C (n = 2) by cathepsin D. ( C ) Cathepsin-D-mediated conversion of pro-VEGF-D into mature VEGF-D (left panel), and rapid activation of ΔNΔC-VEGF-D (a mature form of VEGF-D translated from a truncated cDNA, right panel). ( D ) Cleavage of pro-VEGF-D by KLK3. Note that, KLK3 cleaves VEGF-D between the VEGF homology domain and the N-terminal propeptide, but also between the VEGF homology domain and the C-terminal propeptide (for a detailed breakdown of the cleavage products visible in this overlay and the individual exposures, see ) (n = 2). 10.7554/eLife.44478.021 Figure 6—source data 1. Quantification of the cleavage of pro-VEGF-C and mature VEGF-C by cathepsin D.

    Journal: eLife

    Article Title: KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D

    doi: 10.7554/eLife.44478

    Figure Lengend Snippet: ( A ) Cleavage of VEGF-C by coincubation of pro-VEGF-C with cathepsin D (left panel) and secondary activation of ΔNΔC-VEGF-C (a mature form of VEGF-C translated from a truncated cDNA, right panel). ( B ) Quantification of the cleavage of pro-VEGF-C (n = 3) and ΔNΔC-VEGF-C (n = 2) by cathepsin D. ( C ) Cathepsin-D-mediated conversion of pro-VEGF-D into mature VEGF-D (left panel), and rapid activation of ΔNΔC-VEGF-D (a mature form of VEGF-D translated from a truncated cDNA, right panel). ( D ) Cleavage of pro-VEGF-D by KLK3. Note that, KLK3 cleaves VEGF-D between the VEGF homology domain and the N-terminal propeptide, but also between the VEGF homology domain and the C-terminal propeptide (for a detailed breakdown of the cleavage products visible in this overlay and the individual exposures, see ) (n = 2). 10.7554/eLife.44478.021 Figure 6—source data 1. Quantification of the cleavage of pro-VEGF-C and mature VEGF-C by cathepsin D.

    Article Snippet: Recombinant protein , Cathepsin D (CATD) , R and D Systems/ Biotechne , 1014-AS , .

    Techniques: Activation Assay

    Shown are the results of Ba/F3-VEGFR/EpoR assays used to evaluate the receptor-activating properties of cathepsin D- and KLK3- cleaved proteins. Cathepsin D-cleaved VEGF-C activity in the ( A ) Ba/F3-VEGFR-3/EpoR assay and ( B ) Ba/F3-VEGFR-2/EpoR assay. ( C ) Mature VEGF-D after secondary activation with cathepsin D in the Ba/F3-VEGFR-3/EpoR assay. ( D ) The minor form of mature VEGF-D generated by cathepsin D-cleavage is less active than the major mature form in the Ba/F3-VEGFR-2/EpoR assay. ( E ) KLK3 activation of VEGF-D increases its potency in the Ba/F3-VEGFR-2/EpoR assay. ( F ) The secondary activation of mature VEGF-C with cathepsin D led to a small decrease in the response of Ba/F3-VEGFR-2/EpoR cells (n = 2). Error bars indicate SD. 10.7554/eLife.44478.025 Figure 7—source data 1. Ba/F3 assay showing the receptor-activating properties of cathepsin D-cleaved VEGF-C and VEGF-D.

    Journal: eLife

    Article Title: KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D

    doi: 10.7554/eLife.44478

    Figure Lengend Snippet: Shown are the results of Ba/F3-VEGFR/EpoR assays used to evaluate the receptor-activating properties of cathepsin D- and KLK3- cleaved proteins. Cathepsin D-cleaved VEGF-C activity in the ( A ) Ba/F3-VEGFR-3/EpoR assay and ( B ) Ba/F3-VEGFR-2/EpoR assay. ( C ) Mature VEGF-D after secondary activation with cathepsin D in the Ba/F3-VEGFR-3/EpoR assay. ( D ) The minor form of mature VEGF-D generated by cathepsin D-cleavage is less active than the major mature form in the Ba/F3-VEGFR-2/EpoR assay. ( E ) KLK3 activation of VEGF-D increases its potency in the Ba/F3-VEGFR-2/EpoR assay. ( F ) The secondary activation of mature VEGF-C with cathepsin D led to a small decrease in the response of Ba/F3-VEGFR-2/EpoR cells (n = 2). Error bars indicate SD. 10.7554/eLife.44478.025 Figure 7—source data 1. Ba/F3 assay showing the receptor-activating properties of cathepsin D-cleaved VEGF-C and VEGF-D.

    Article Snippet: Recombinant protein , Cathepsin D (CATD) , R and D Systems/ Biotechne , 1014-AS , .

    Techniques: Activity Assay, Activation Assay, Generated

    Pro-VEGF-D cleaved by cathepsin D stimulated the phosphorylation of VEGFR-2 expressed in PAE cells at 40 ng/ml and 80 ng/ml concentrations.

    Journal: eLife

    Article Title: KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D

    doi: 10.7554/eLife.44478

    Figure Lengend Snippet: Pro-VEGF-D cleaved by cathepsin D stimulated the phosphorylation of VEGFR-2 expressed in PAE cells at 40 ng/ml and 80 ng/ml concentrations.

    Article Snippet: Recombinant protein , Cathepsin D (CATD) , R and D Systems/ Biotechne , 1014-AS , .

    Techniques:

    ( A ) Shown are the immunofluorescent stainings of the blood and lymphatic vessels in skeletal muscle transduced with recombinant adeno-associated virus subtype 9 (AAV9) encoding the KLK3- or the cathepsin D (CATD)-form of VEGF-C. Quantification of ( B ) Lyve-1 positive stained area and ( C ) CD31 positive stained area in AAV9 transduced tibialis anterior muscle. Data are presented as mean ± SEM, n = 4, one-way ANOVA with Tukey’s post hoc test, ***p<0.001, *p<0.05. Scale bar, 100 µm. (see also ). 10.7554/eLife.44478.029 Figure 8—source data 1. In vivo quantification of lymphangiogenesis and angiogenesis induced by KLK3- and cathepsin D-forms of VEGF-C.

    Journal: eLife

    Article Title: KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D

    doi: 10.7554/eLife.44478

    Figure Lengend Snippet: ( A ) Shown are the immunofluorescent stainings of the blood and lymphatic vessels in skeletal muscle transduced with recombinant adeno-associated virus subtype 9 (AAV9) encoding the KLK3- or the cathepsin D (CATD)-form of VEGF-C. Quantification of ( B ) Lyve-1 positive stained area and ( C ) CD31 positive stained area in AAV9 transduced tibialis anterior muscle. Data are presented as mean ± SEM, n = 4, one-way ANOVA with Tukey’s post hoc test, ***p<0.001, *p<0.05. Scale bar, 100 µm. (see also ). 10.7554/eLife.44478.029 Figure 8—source data 1. In vivo quantification of lymphangiogenesis and angiogenesis induced by KLK3- and cathepsin D-forms of VEGF-C.

    Article Snippet: Recombinant protein , Cathepsin D (CATD) , R and D Systems/ Biotechne , 1014-AS , .

    Techniques: Transduction, Recombinant, Virus, Staining, In Vivo

    Comparison of VEGF-C mRNA levels in TA muscle transduced with AAV9 encoding for the different forms of mature VEGF-C generated by ADAMTS3 (Pos Ctrl), cathepsin D (CATD-form) and KLK3 (KLK3-form). Data are presented as mean ± SEM.

    Journal: eLife

    Article Title: KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D

    doi: 10.7554/eLife.44478

    Figure Lengend Snippet: Comparison of VEGF-C mRNA levels in TA muscle transduced with AAV9 encoding for the different forms of mature VEGF-C generated by ADAMTS3 (Pos Ctrl), cathepsin D (CATD-form) and KLK3 (KLK3-form). Data are presented as mean ± SEM.

    Article Snippet: Recombinant protein , Cathepsin D (CATD) , R and D Systems/ Biotechne , 1014-AS , .

    Techniques: Comparison, Transduction, Generated

    Journal: eLife

    Article Title: KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D

    doi: 10.7554/eLife.44478

    Figure Lengend Snippet:

    Article Snippet: Recombinant protein , Cathepsin D (CATD) , R and D Systems/ Biotechne , 1014-AS , .

    Techniques: Expressing, Transfection, Construct, Mutagenesis, Recombinant, Virus, Positive Control, Negative Control, Transformation Assay, Neutralization, Enzyme-linked Immunosorbent Assay, Plasmid Preparation