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recombinant psgl 1  (Sino Biological)


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    Structured Review

    Sino Biological recombinant psgl 1
    Cathepsin K (CTSK) tolerates glycans near the cleavage site. A, cleavage motif of CTSK was generated from mass spectrometry analysis of ( left ) glycopeptides, ( center ) nonmodified peptides, and ( right ) modified and nonmodified peptides generated from CTSK digestion of purified and recombinant mucins and nonmucin glycoproteins, followed by trypsin digestion (see the section). The bar graphs on top of the glycopeptide cleavage motif indicate the frequency of O -glycosylation at each threonine and serine residue at that position. B, top, visualization of CTSK cleavage sites in recombinant MUC1 residues 24–47. The sialylated core-1 glycan at specific resides indicates that glycans were seen at those sites. This specific glycan was seen often in the dataset, but its depiction here is only intended to indicate glycosites, not to represent the diversity of all glycans detected at each glycosite in the dataset. Purple diamond , sialic acid; yellow circle , galactose; yellow square , N-acetylgalactosamine; and yellow circle , glycosylation site. Colored bars represent individual detected peptide sequences from CTSK cleavage only, with any shared peptides with chymotrypsin removed. Bottom, annotated spectrum for the indicated MUC1 O -glycopeptide. C, top, visualization of CTSK cleavage sites in recombinant P-selectin glycoprotein ligand-1 <t>(PSGL-1)</t> residues 148 to 197, represented as in ( B ), but this time from the tryptic + CTSK dataset, with all tryptic cleavage sites removed. Bottom, annotated spectrum for the indicated PSGL-1 O -glycopeptide. MUC, mucin.
    Recombinant Psgl 1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant psgl 1/product/Sino Biological
    Average 94 stars, based on 5 article reviews
    recombinant psgl 1 - by Bioz Stars, 2026-05
    94/100 stars

    Images

    1) Product Images from "The protease cathepsin K can debulk the cancer glycocalyx"

    Article Title: The protease cathepsin K can debulk the cancer glycocalyx

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2026.111206

    Cathepsin K (CTSK) tolerates glycans near the cleavage site. A, cleavage motif of CTSK was generated from mass spectrometry analysis of ( left ) glycopeptides, ( center ) nonmodified peptides, and ( right ) modified and nonmodified peptides generated from CTSK digestion of purified and recombinant mucins and nonmucin glycoproteins, followed by trypsin digestion (see the section). The bar graphs on top of the glycopeptide cleavage motif indicate the frequency of O -glycosylation at each threonine and serine residue at that position. B, top, visualization of CTSK cleavage sites in recombinant MUC1 residues 24–47. The sialylated core-1 glycan at specific resides indicates that glycans were seen at those sites. This specific glycan was seen often in the dataset, but its depiction here is only intended to indicate glycosites, not to represent the diversity of all glycans detected at each glycosite in the dataset. Purple diamond , sialic acid; yellow circle , galactose; yellow square , N-acetylgalactosamine; and yellow circle , glycosylation site. Colored bars represent individual detected peptide sequences from CTSK cleavage only, with any shared peptides with chymotrypsin removed. Bottom, annotated spectrum for the indicated MUC1 O -glycopeptide. C, top, visualization of CTSK cleavage sites in recombinant P-selectin glycoprotein ligand-1 (PSGL-1) residues 148 to 197, represented as in ( B ), but this time from the tryptic + CTSK dataset, with all tryptic cleavage sites removed. Bottom, annotated spectrum for the indicated PSGL-1 O -glycopeptide. MUC, mucin.
    Figure Legend Snippet: Cathepsin K (CTSK) tolerates glycans near the cleavage site. A, cleavage motif of CTSK was generated from mass spectrometry analysis of ( left ) glycopeptides, ( center ) nonmodified peptides, and ( right ) modified and nonmodified peptides generated from CTSK digestion of purified and recombinant mucins and nonmucin glycoproteins, followed by trypsin digestion (see the section). The bar graphs on top of the glycopeptide cleavage motif indicate the frequency of O -glycosylation at each threonine and serine residue at that position. B, top, visualization of CTSK cleavage sites in recombinant MUC1 residues 24–47. The sialylated core-1 glycan at specific resides indicates that glycans were seen at those sites. This specific glycan was seen often in the dataset, but its depiction here is only intended to indicate glycosites, not to represent the diversity of all glycans detected at each glycosite in the dataset. Purple diamond , sialic acid; yellow circle , galactose; yellow square , N-acetylgalactosamine; and yellow circle , glycosylation site. Colored bars represent individual detected peptide sequences from CTSK cleavage only, with any shared peptides with chymotrypsin removed. Bottom, annotated spectrum for the indicated MUC1 O -glycopeptide. C, top, visualization of CTSK cleavage sites in recombinant P-selectin glycoprotein ligand-1 (PSGL-1) residues 148 to 197, represented as in ( B ), but this time from the tryptic + CTSK dataset, with all tryptic cleavage sites removed. Bottom, annotated spectrum for the indicated PSGL-1 O -glycopeptide. MUC, mucin.

    Techniques Used: Generated, Mass Spectrometry, Modification, Purification, Recombinant, Glycoproteomics, Residue



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    Cathepsin K (CTSK) tolerates glycans near the cleavage site. A, cleavage motif of CTSK was generated from mass spectrometry analysis of ( left ) glycopeptides, ( center ) nonmodified peptides, and ( right ) modified and nonmodified peptides generated from CTSK digestion of purified and recombinant mucins and nonmucin glycoproteins, followed by trypsin digestion (see the section). The bar graphs on top of the glycopeptide cleavage motif indicate the frequency of O -glycosylation at each threonine and serine residue at that position. B, top, visualization of CTSK cleavage sites in recombinant MUC1 residues 24–47. The sialylated core-1 glycan at specific resides indicates that glycans were seen at those sites. This specific glycan was seen often in the dataset, but its depiction here is only intended to indicate glycosites, not to represent the diversity of all glycans detected at each glycosite in the dataset. Purple diamond , sialic acid; yellow circle , galactose; yellow square , N-acetylgalactosamine; and yellow circle , glycosylation site. Colored bars represent individual detected peptide sequences from CTSK cleavage only, with any shared peptides with chymotrypsin removed. Bottom, annotated spectrum for the indicated MUC1 O -glycopeptide. C, top, visualization of CTSK cleavage sites in recombinant P-selectin glycoprotein ligand-1 <t>(PSGL-1)</t> residues 148 to 197, represented as in ( B ), but this time from the tryptic + CTSK dataset, with all tryptic cleavage sites removed. Bottom, annotated spectrum for the indicated PSGL-1 O -glycopeptide. MUC, mucin.
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    Image Search Results


    Cathepsin K (CTSK) tolerates glycans near the cleavage site. A, cleavage motif of CTSK was generated from mass spectrometry analysis of ( left ) glycopeptides, ( center ) nonmodified peptides, and ( right ) modified and nonmodified peptides generated from CTSK digestion of purified and recombinant mucins and nonmucin glycoproteins, followed by trypsin digestion (see the section). The bar graphs on top of the glycopeptide cleavage motif indicate the frequency of O -glycosylation at each threonine and serine residue at that position. B, top, visualization of CTSK cleavage sites in recombinant MUC1 residues 24–47. The sialylated core-1 glycan at specific resides indicates that glycans were seen at those sites. This specific glycan was seen often in the dataset, but its depiction here is only intended to indicate glycosites, not to represent the diversity of all glycans detected at each glycosite in the dataset. Purple diamond , sialic acid; yellow circle , galactose; yellow square , N-acetylgalactosamine; and yellow circle , glycosylation site. Colored bars represent individual detected peptide sequences from CTSK cleavage only, with any shared peptides with chymotrypsin removed. Bottom, annotated spectrum for the indicated MUC1 O -glycopeptide. C, top, visualization of CTSK cleavage sites in recombinant P-selectin glycoprotein ligand-1 (PSGL-1) residues 148 to 197, represented as in ( B ), but this time from the tryptic + CTSK dataset, with all tryptic cleavage sites removed. Bottom, annotated spectrum for the indicated PSGL-1 O -glycopeptide. MUC, mucin.

    Journal: The Journal of Biological Chemistry

    Article Title: The protease cathepsin K can debulk the cancer glycocalyx

    doi: 10.1016/j.jbc.2026.111206

    Figure Lengend Snippet: Cathepsin K (CTSK) tolerates glycans near the cleavage site. A, cleavage motif of CTSK was generated from mass spectrometry analysis of ( left ) glycopeptides, ( center ) nonmodified peptides, and ( right ) modified and nonmodified peptides generated from CTSK digestion of purified and recombinant mucins and nonmucin glycoproteins, followed by trypsin digestion (see the section). The bar graphs on top of the glycopeptide cleavage motif indicate the frequency of O -glycosylation at each threonine and serine residue at that position. B, top, visualization of CTSK cleavage sites in recombinant MUC1 residues 24–47. The sialylated core-1 glycan at specific resides indicates that glycans were seen at those sites. This specific glycan was seen often in the dataset, but its depiction here is only intended to indicate glycosites, not to represent the diversity of all glycans detected at each glycosite in the dataset. Purple diamond , sialic acid; yellow circle , galactose; yellow square , N-acetylgalactosamine; and yellow circle , glycosylation site. Colored bars represent individual detected peptide sequences from CTSK cleavage only, with any shared peptides with chymotrypsin removed. Bottom, annotated spectrum for the indicated MUC1 O -glycopeptide. C, top, visualization of CTSK cleavage sites in recombinant P-selectin glycoprotein ligand-1 (PSGL-1) residues 148 to 197, represented as in ( B ), but this time from the tryptic + CTSK dataset, with all tryptic cleavage sites removed. Bottom, annotated spectrum for the indicated PSGL-1 O -glycopeptide. MUC, mucin.

    Article Snippet: Purified recombinant PSGL-1 (Sino Biological; 13863-H08H) was labeled with IRDye 800CW NHS Ester (LI-COR Biosciences) following the manufacturer’s recommendations.

    Techniques: Generated, Mass Spectrometry, Modification, Purification, Recombinant, Glycoproteomics, Residue