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synthetic β–casein peptide  (AnaSpec)

 
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    Structured Review

    AnaSpec synthetic β–casein peptide
    Mass spectra of the <t>tetraphosphorylated</t> <t>β‐casein</t> peptide in the presence of uranyl, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. C) Detail of mass spectra displaying the isotope distributions of the three major photocleavage products. D) Sequence of the tetraphosphorylated β‐casein peptide. The observed cleavages are indicated with solid lines, with residue number (above) and mass (below). Int. Std.=internal standard (neurotensin).
    Synthetic β–Casein Peptide, supplied by AnaSpec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/synthetic+%CE%B2%E2%80%93casein+peptide/synthetic+%CE%B2+casein+peptide/pmc05488209-118-10-19
    Average 90 stars, based on 1 article reviews
    synthetic β–casein peptide - by Bioz Stars, 2026-10
    90/100 stars

    Images

    1) Product Images from "Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products"

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products

    Journal: Chembiochem

    doi: 10.1002/cbic.201700103

    Mass spectra of the tetraphosphorylated β‐casein peptide in the presence of uranyl, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. C) Detail of mass spectra displaying the isotope distributions of the three major photocleavage products. D) Sequence of the tetraphosphorylated β‐casein peptide. The observed cleavages are indicated with solid lines, with residue number (above) and mass (below). Int. Std.=internal standard (neurotensin).
    Figure Legend Snippet: Mass spectra of the tetraphosphorylated β‐casein peptide in the presence of uranyl, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. C) Detail of mass spectra displaying the isotope distributions of the three major photocleavage products. D) Sequence of the tetraphosphorylated β‐casein peptide. The observed cleavages are indicated with solid lines, with residue number (above) and mass (below). Int. Std.=internal standard (neurotensin).

    Techniques Used: Irradiation, Sequencing, Residue

    CID spectra of peptides (1–9), (1–14) and (1–16) formed by uranyl photocleavage of the β‐casein peptide. Mass spectra of photocleavage products with precursor masses: A) m / z 549.30, 2+ (1097.6 Da), B) m / z 812.93, 2+ (1624.9 Da), and C) m / z 953.47, 2+ (1904.9 Da). Sequences of the respective photocleavage products are shown below each spectrum, indicating the identified b‐ and y‐ions.
    Figure Legend Snippet: CID spectra of peptides (1–9), (1–14) and (1–16) formed by uranyl photocleavage of the β‐casein peptide. Mass spectra of photocleavage products with precursor masses: A) m / z 549.30, 2+ (1097.6 Da), B) m / z 812.93, 2+ (1624.9 Da), and C) m / z 953.47, 2+ (1904.9 Da). Sequences of the respective photocleavage products are shown below each spectrum, indicating the identified b‐ and y‐ions.

    Techniques Used:

    Mass spectra obtained from the β‐casein peptide incubated with uranyl in an essentially oxygen‐free environment, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. The experiment was carried out in a glovebox (oxygen <1 ppm). Prior to UV irradiation the samples were degassed by bubbling xenon through the samples for 5 min. Finally the samples were desalted and the mass was analysed by MALDI‐MS. Int. Std.=internal standard (neurotensin).
    Figure Legend Snippet: Mass spectra obtained from the β‐casein peptide incubated with uranyl in an essentially oxygen‐free environment, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. The experiment was carried out in a glovebox (oxygen <1 ppm). Prior to UV irradiation the samples were degassed by bubbling xenon through the samples for 5 min. Finally the samples were desalted and the mass was analysed by MALDI‐MS. Int. Std.=internal standard (neurotensin).

    Techniques Used: Incubation, Irradiation

    Related Articles

    Irradiation:

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products
    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).

    Sequencing:

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products
    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).

    Residue:

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products
    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).

    Incubation:

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products
    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).



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    Mass spectra of the <t>tetraphosphorylated</t> <t>β‐casein</t> peptide in the presence of uranyl, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. C) Detail of mass spectra displaying the isotope distributions of the three major photocleavage products. D) Sequence of the tetraphosphorylated β‐casein peptide. The observed cleavages are indicated with solid lines, with residue number (above) and mass (below). Int. Std.=internal standard (neurotensin).
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    Image Search Results


    Mass spectra of the tetraphosphorylated β‐casein peptide in the presence of uranyl, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. C) Detail of mass spectra displaying the isotope distributions of the three major photocleavage products. D) Sequence of the tetraphosphorylated β‐casein peptide. The observed cleavages are indicated with solid lines, with residue number (above) and mass (below). Int. Std.=internal standard (neurotensin).

    Journal: Chembiochem

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products

    doi: 10.1002/cbic.201700103

    Figure Lengend Snippet: Mass spectra of the tetraphosphorylated β‐casein peptide in the presence of uranyl, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. C) Detail of mass spectra displaying the isotope distributions of the three major photocleavage products. D) Sequence of the tetraphosphorylated β‐casein peptide. The observed cleavages are indicated with solid lines, with residue number (above) and mass (below). Int. Std.=internal standard (neurotensin).

    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).

    Techniques: Irradiation, Sequencing, Residue

    CID spectra of peptides (1–9), (1–14) and (1–16) formed by uranyl photocleavage of the β‐casein peptide. Mass spectra of photocleavage products with precursor masses: A) m / z 549.30, 2+ (1097.6 Da), B) m / z 812.93, 2+ (1624.9 Da), and C) m / z 953.47, 2+ (1904.9 Da). Sequences of the respective photocleavage products are shown below each spectrum, indicating the identified b‐ and y‐ions.

    Journal: Chembiochem

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products

    doi: 10.1002/cbic.201700103

    Figure Lengend Snippet: CID spectra of peptides (1–9), (1–14) and (1–16) formed by uranyl photocleavage of the β‐casein peptide. Mass spectra of photocleavage products with precursor masses: A) m / z 549.30, 2+ (1097.6 Da), B) m / z 812.93, 2+ (1624.9 Da), and C) m / z 953.47, 2+ (1904.9 Da). Sequences of the respective photocleavage products are shown below each spectrum, indicating the identified b‐ and y‐ions.

    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).

    Techniques:

    Mass spectra obtained from the β‐casein peptide incubated with uranyl in an essentially oxygen‐free environment, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. The experiment was carried out in a glovebox (oxygen <1 ppm). Prior to UV irradiation the samples were degassed by bubbling xenon through the samples for 5 min. Finally the samples were desalted and the mass was analysed by MALDI‐MS. Int. Std.=internal standard (neurotensin).

    Journal: Chembiochem

    Article Title: Uranyl Photocleavage of Phosphopeptides Yields Truncated C‐Terminally Amidated Peptide Products

    doi: 10.1002/cbic.201700103

    Figure Lengend Snippet: Mass spectra obtained from the β‐casein peptide incubated with uranyl in an essentially oxygen‐free environment, A) without UV and B) after UV irradiation. Asterisked peaks are MALDI‐induced neutral losses of H 3 PO 4 from the intact peptide. The experiment was carried out in a glovebox (oxygen <1 ppm). Prior to UV irradiation the samples were degassed by bubbling xenon through the samples for 5 min. Finally the samples were desalted and the mass was analysed by MALDI‐MS. Int. Std.=internal standard (neurotensin).

    Article Snippet: The reactions were carried out in low‐binding Eppendorf tubes containing synthetic β‐casein peptide (10 μ m >95 % purity; AnaSpec), UO 2 (NO 3 ) 2 (50 μ m) and neurotensin (0.5 μ m; internal standard, >90 % purity; Sigma–Aldrich) in Tris ⋅ HCl (20 m m , pH 8.0).

    Techniques: Incubation, Irradiation