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rabbit polyclonal antibody against human transferrin  (Agilent technologies)


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    Structured Review

    Agilent technologies rabbit polyclonal antibody against human transferrin
    Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of <t>transferrin.</t>
    Rabbit Polyclonal Antibody Against Human Transferrin, supplied by Agilent technologies, 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/rabbit+polyclonal+antibody+against+human+transferrin/pmc07242785-30-8-14
    Average 90 stars, based on 1 article reviews
    rabbit polyclonal antibody against human transferrin - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation"

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation

    Journal: Mass Spectrometry

    doi: 10.5702/massspectrometry.A0084

    Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of transferrin.
    Figure Legend Snippet: Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of transferrin.

    Techniques Used:

    Fig. 3. MALDI linear TOF mass spectrum of tryptic peptides of transferrin obtained from a healthy individual. The peaks indicated by sequence numbers in parentheses are ions without glycosylation sites. Their sequences are AIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSK (51–88) and AVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFK (149–193). Glycoforms at site-1 and site-2 are displayed in the lower and higher mass regions, respectively.
    Figure Legend Snippet: Fig. 3. MALDI linear TOF mass spectrum of tryptic peptides of transferrin obtained from a healthy individual. The peaks indicated by sequence numbers in parentheses are ions without glycosylation sites. Their sequences are AIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSK (51–88) and AVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFK (149–193). Glycoforms at site-1 and site-2 are displayed in the lower and higher mass regions, respectively.

    Techniques Used: Sequencing

    Fig. 4. MALDI reflectron TOF mass spectra of tryptic peptides of transferrin. (a) CDG-I patient. Arrows indicate diagnostic ions. This patient is a compound heterozygote for ALG1 mutations and has a mutation in the SSR4 gene which is also among the candidate causes of CDG-I type abnormalities. (b) Healthy individual. Broken arrows indicate the positions of diagnostic ions; it is noteworthy that a small peak at m / z 2525.1 is observed in this unaffected subject.
    Figure Legend Snippet: Fig. 4. MALDI reflectron TOF mass spectra of tryptic peptides of transferrin. (a) CDG-I patient. Arrows indicate diagnostic ions. This patient is a compound heterozygote for ALG1 mutations and has a mutation in the SSR4 gene which is also among the candidate causes of CDG-I type abnormalities. (b) Healthy individual. Broken arrows indicate the positions of diagnostic ions; it is noteworthy that a small peak at m / z 2525.1 is observed in this unaffected subject.

    Techniques Used: Diagnostic Assay, Mutagenesis

    Fig. 5. MALDI linear TOF mass spectrum of tryptic peptides of transferrin from patients with various types of CDG-II.
    Figure Legend Snippet: Fig. 5. MALDI linear TOF mass spectrum of tryptic peptides of transferrin from patients with various types of CDG-II.

    Techniques Used:

    Related Articles

    Affinity Column:

    Article Title: L-Fucose treatment of FUT8-CDG
    Article Snippet: .. Briefly, an affinity column for transferrin was prepared using a rabbit polyclonal antibody against human transferrin (Dako, Glostrup, Denmark) and a ligand-coupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, NJ, USA). .. For IgG, a protein G-coupled Sepharose column was purchased from GE Healthcare.

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation
    Article Snippet: .. Briefly, an affinity column was prepared using a rabbit polyclonal antibody against human transferrin (DAKO, Denmark) and a ligand-coupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, Piscataway, NJ, USA), and the antibody-coupled Sepharose was recovered from the column. ..

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation
    Article Snippet: .. 12) Briefly, an affinity column was prepared using rabbit polyclonal antibody against human transferrin (DAKO, Denmark) and a ligandcoupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, Piscataway, NJ), and the antibody-coupled Sepharose was recovered from the column. ..

    Purification:

    Article Title: Clinical and molecular findings in three Japanese patients with N -acetylneuraminic acid synthetase-congenital disorder of glycosylation (NANS-CDG)
    Article Snippet: .. In brief, each protein was purified from serum by immunoaffinity with rabbit polyclonal antibody against human transferrin (Dako) or goat polyclonal antibody against human apolipoprotein C-III (Academy Bio-Medical Co), and was subjected to liquid chromatography-ESI–MS using a reversed-phase, C4 for transferrin and C8 for apolipoprotein C-III, minicolumn and an API4500 quadrupole mass spectrometer (Sciex). .. The obtained mass spectrum of multiply-charged ions was transformed into a single-charge spectrum using a Promass protein deconvolution software (ThermoFisher Scientific).

    Chromatography:

    Article Title: Clinical and molecular findings in three Japanese patients with N -acetylneuraminic acid synthetase-congenital disorder of glycosylation (NANS-CDG)
    Article Snippet: .. In brief, each protein was purified from serum by immunoaffinity with rabbit polyclonal antibody against human transferrin (Dako) or goat polyclonal antibody against human apolipoprotein C-III (Academy Bio-Medical Co), and was subjected to liquid chromatography-ESI–MS using a reversed-phase, C4 for transferrin and C8 for apolipoprotein C-III, minicolumn and an API4500 quadrupole mass spectrometer (Sciex). .. The obtained mass spectrum of multiply-charged ions was transformed into a single-charge spectrum using a Promass protein deconvolution software (ThermoFisher Scientific).

    Mass Spectrometry:

    Article Title: Clinical and molecular findings in three Japanese patients with N -acetylneuraminic acid synthetase-congenital disorder of glycosylation (NANS-CDG)
    Article Snippet: .. In brief, each protein was purified from serum by immunoaffinity with rabbit polyclonal antibody against human transferrin (Dako) or goat polyclonal antibody against human apolipoprotein C-III (Academy Bio-Medical Co), and was subjected to liquid chromatography-ESI–MS using a reversed-phase, C4 for transferrin and C8 for apolipoprotein C-III, minicolumn and an API4500 quadrupole mass spectrometer (Sciex). .. The obtained mass spectrum of multiply-charged ions was transformed into a single-charge spectrum using a Promass protein deconvolution software (ThermoFisher Scientific).



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    Agilent technologies rabbit polyclonal antibody against human transferrin
    Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of <t>transferrin.</t>
    Rabbit Polyclonal Antibody Against Human Transferrin, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies polyclonal rabbit antibodies against human transferrin
    Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of <t>transferrin.</t>
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    Image Search Results


    Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of transferrin.

    Journal: Mass Spectrometry

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation

    doi: 10.5702/massspectrometry.A0084

    Figure Lengend Snippet: Fig. 2. Sequences of the tryptic glycopeptide and the major glycoforms of transferrin.

    Article Snippet: Briefly, an affinity column was prepared using a rabbit polyclonal antibody against human transferrin (DAKO, Denmark) and a ligand-coupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, Piscataway, NJ, USA), and the antibody-coupled Sepharose was recovered from the column.

    Techniques:

    Fig. 3. MALDI linear TOF mass spectrum of tryptic peptides of transferrin obtained from a healthy individual. The peaks indicated by sequence numbers in parentheses are ions without glycosylation sites. Their sequences are AIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSK (51–88) and AVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFK (149–193). Glycoforms at site-1 and site-2 are displayed in the lower and higher mass regions, respectively.

    Journal: Mass Spectrometry

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation

    doi: 10.5702/massspectrometry.A0084

    Figure Lengend Snippet: Fig. 3. MALDI linear TOF mass spectrum of tryptic peptides of transferrin obtained from a healthy individual. The peaks indicated by sequence numbers in parentheses are ions without glycosylation sites. Their sequences are AIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSK (51–88) and AVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFK (149–193). Glycoforms at site-1 and site-2 are displayed in the lower and higher mass regions, respectively.

    Article Snippet: Briefly, an affinity column was prepared using a rabbit polyclonal antibody against human transferrin (DAKO, Denmark) and a ligand-coupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, Piscataway, NJ, USA), and the antibody-coupled Sepharose was recovered from the column.

    Techniques: Sequencing

    Fig. 4. MALDI reflectron TOF mass spectra of tryptic peptides of transferrin. (a) CDG-I patient. Arrows indicate diagnostic ions. This patient is a compound heterozygote for ALG1 mutations and has a mutation in the SSR4 gene which is also among the candidate causes of CDG-I type abnormalities. (b) Healthy individual. Broken arrows indicate the positions of diagnostic ions; it is noteworthy that a small peak at m / z 2525.1 is observed in this unaffected subject.

    Journal: Mass Spectrometry

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation

    doi: 10.5702/massspectrometry.A0084

    Figure Lengend Snippet: Fig. 4. MALDI reflectron TOF mass spectra of tryptic peptides of transferrin. (a) CDG-I patient. Arrows indicate diagnostic ions. This patient is a compound heterozygote for ALG1 mutations and has a mutation in the SSR4 gene which is also among the candidate causes of CDG-I type abnormalities. (b) Healthy individual. Broken arrows indicate the positions of diagnostic ions; it is noteworthy that a small peak at m / z 2525.1 is observed in this unaffected subject.

    Article Snippet: Briefly, an affinity column was prepared using a rabbit polyclonal antibody against human transferrin (DAKO, Denmark) and a ligand-coupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, Piscataway, NJ, USA), and the antibody-coupled Sepharose was recovered from the column.

    Techniques: Diagnostic Assay, Mutagenesis

    Fig. 5. MALDI linear TOF mass spectrum of tryptic peptides of transferrin from patients with various types of CDG-II.

    Journal: Mass Spectrometry

    Article Title: Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation

    doi: 10.5702/massspectrometry.A0084

    Figure Lengend Snippet: Fig. 5. MALDI linear TOF mass spectrum of tryptic peptides of transferrin from patients with various types of CDG-II.

    Article Snippet: Briefly, an affinity column was prepared using a rabbit polyclonal antibody against human transferrin (DAKO, Denmark) and a ligand-coupling Sepharose column (HiTrap NHS-activated HP, GE Healthcare, Piscataway, NJ, USA), and the antibody-coupled Sepharose was recovered from the column.

    Techniques: