proteinase k (Merck KGaA)
Structured Review

Proteinase K, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 86 stars, based on 1 article reviews
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Images
1) Product Images from "Elucidating the Immune Evasion Mechanisms of Borrelia mayonii, the Causative Agent of Lyme Disease"
Article Title: Elucidating the Immune Evasion Mechanisms of Borrelia mayonii, the Causative Agent of Lyme Disease
Journal: Frontiers in Immunology
doi: 10.3389/fimmu.2019.02722

Figure Legend Snippet: Identification and surface exposure of FH/FHL-1-binding proteins in B. mayonii MN14-1420. (A,B) Detection of FH/FHL-1-binding proteins by Far Western blot analysis using NHS as source of FH and purified FHL-1 (750 ng/ml). Cell lysates obtained from B. mayonii MN14-1420, B. burgdorferi LW2, B. burgdorferi B31, B. burgdorferi PKa-1, B. garinii G1, and transformant G1/pCspA_Bmayo were separated by 10% Tris/tricine-SDS-PAGE and transferred onto a nitrocellulose membrane. Flagellin (FlaB) was detected with the monoclonal antibody L41 1C11. The FH-binding proteins (A) were visualized by applying an anti-FH antiserum and FHL-1-binding proteins (B) were detected by using an anti-CCP1-4 antiserum. The corresponding to CspA protein of B. mayonii (Bm) MN14-1420, CspA of B. burgdorferi (Bb) LW2, CspZ, ErpP, and ErpA of B. burgdorferi s.s. are indicated at the right. (C) in situ protease accessibility assay. Native spirochetes were incubated with or without proteinase K or trypsin, then lysed by sonication and total proteins were separated by 10% Tris/tricine-SDS-PAGE. The band corresponding to CspA of B. mayonii is indicated on the right. The mobilities of molecular mass standards are indicated on the left. A full scan of the original membranes is presented in Supplementary Figure 5 .
Techniques Used: Binding Assay, Far Western Blot, Purification, SDS Page, In Situ, Incubation, Sonication
2) Product Images from "Structure and Specific Activity of Macrophage-Stimulating Lipopeptides from Mycoplasma hyorhinis"
Article Title: Structure and Specific Activity of Macrophage-Stimulating Lipopeptides from Mycoplasma hyorhinis
Journal: Infection and Immunity
doi:

Figure Legend Snippet: HPLC of octyl glucoside-extracted MSA from M. hyorhinis . MSA, as determined by the nitric oxide release assay (solid line), was eluted with a 2-propanol gradient (straight dashed line). The UV trace at 256 nm is shown as a fainter dashed line. (A) A sample from an octyl glucoside extract of M. hyorhinis clone VIII-23 containing 5.5 mg of protein with 2 × 10 7 U of MSA was applied to a 10- by 250-mm RP18 reversed-phase column. (B) Material eluting in peak 1 was treated with proteinase K and rechromatographed on a 4- by 250-mm RP18 column.
Techniques Used: High Performance Liquid Chromatography, Release Assay
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