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ImmunohistochemistryAntibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
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- Product number
- ABIN966421 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Integrin alpha V (ITGAV) (C-Term) antibody
- Antibody type
- Polyclonal
- Antigen
- Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human ITGAV (Integrin alpha-V precursor)
- Description
- Purified by antigen-specific affinity chromatography.
- Reactivity
- Human, Mouse, Chicken/Avian
- Host
- Rabbit
- Epitope
- C-Term
- Vial size
- 0.1 mg
- Storage
- -20°C
Submitted references Mass spectrometric based mapping of the disulfide bonding patterns of integrin alpha chains.
Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
Crystal structure of the extracellular segment of integrin alpha Vbeta3.
A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells.
cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors.
Krokhin OV, Cheng K, Sousa SL, Ens W, Standing KG, Wilkins JA
Biochemistry 2003 Nov 11;42(44):12950-9
Biochemistry 2003 Nov 11;42(44):12950-9
Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
Zhang H, Li XJ, Martin DB, Aebersold R
Nature biotechnology 2003 Jun;21(6):660-6
Nature biotechnology 2003 Jun;21(6):660-6
Crystal structure of the extracellular segment of integrin alpha Vbeta3.
Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, Joachimiak A, Goodman SL, Arnaout MA
Science (New York, N.Y.) 2001 Oct 12;294(5541):339-45
Science (New York, N.Y.) 2001 Oct 12;294(5541):339-45
A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells.
Cheresh DA, Smith JW, Cooper HM, Quaranta V
Cell 1989 Apr 7;57(1):59-69
Cell 1989 Apr 7;57(1):59-69
cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors.
Suzuki S, Argraves WS, Pytela R, Arai H, Krusius T, Pierschbacher MD, Ruoslahti E
Proceedings of the National Academy of Sciences of the United States of America 1986 Nov;83(22):8614-8
Proceedings of the National Academy of Sciences of the United States of America 1986 Nov;83(22):8614-8
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