biological source
goat
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized
does not contain
preservative
species reactivity
human
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
ambient
storage temp.
−20°C
Quality Level
General description
Anti-Angiogenin, goat polyclonal, recognizes angiogenin and can neutralize the activity of human recombinant angiogenin. It is validated for ELISA, Western blotting, and neutralization studies.
Immunoaffinity purified goat polyclonal antibody. Recognizes the ~14 kDa angiogenin protein.
Recognizes angiogenin.Antibody Target Gene Symbol: ANG Target Synonym: AI385586, ALS9, Ang1, Ang2, ANGIOGENIN, ANGIOGENIN 2, BRB, BRN, HEL168, MGC140149, MGC22466, MGC71966, RNASE4, RNASE5, Rnase5a Entrez Gene Name: angiogenin, ribonuclease, RNase A family, 5 Hu Entrez ID: 283 Mu Entrez ID: 11727 Rat Entrez ID: 305843, 497229
Immunogen
Human
recombinant, human angiogenin
Application
ELISA (0.5-1 µg/ml)
Immunoblotting (1-2 µg/ml)
Neutralization Studies (EC₅₀= 100-150 µg/µg angiogenin, see comments)
Immunoblotting (1-2 µg/ml)
Neutralization Studies (EC₅₀= 100-150 µg/µg angiogenin, see comments)
Physical form
Lyophilized from 20 mM ammonium bicarbonate, PBS, 100 µg FAF-BSA.
Preparation Note
Reconstitute the lyophilized antibody with sterile PBS, pH 7.4, or sterile 20 mM Tris-saline (20 mM Tris containing 0.15 M NaCl), pH 7.4, to yield a final concentration of 1 mg/ml. Lyophilized antibodies should be resuspended at 4°C with occasional gentle mixing for at least 2 h. Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C. Avoid freeze/thaw cycles of solutions.
Analysis Note
Positive Control
HT-29 cells
HT-29 cells
Other Notes
Shapiro, R. 1998. Biochemistry37, 6847.
Soncin, F., et al. 1997. Biochem. Biophys. Res. Commun.236 604.
Vallee, B.L. and Riordan, J.F. 1997. Cell Mol. Life Sci.53 803.
Moenner, M., et al. 1994. Eur. J. Biochem.226 483.
Hu, G.F., et al. 1993. PNAS.90 1217.
Moroianu, J., et al. 1993. PNAS.90 3815.
Soncin, F. 1992. PNAS.89 2232.
Lee, F.S. and Vallee, B.L. 1989. Biochem. Biophys. Res. Commun.161 121.
Kurachi, K., et al. 1985. Biochemistry24, 5494.
Soncin, F., et al. 1997. Biochem. Biophys. Res. Commun.236 604.
Vallee, B.L. and Riordan, J.F. 1997. Cell Mol. Life Sci.53 803.
Moenner, M., et al. 1994. Eur. J. Biochem.226 483.
Hu, G.F., et al. 1993. PNAS.90 1217.
Moroianu, J., et al. 1993. PNAS.90 3815.
Soncin, F. 1992. PNAS.89 2232.
Lee, F.S. and Vallee, B.L. 1989. Biochem. Biophys. Res. Commun.161 121.
Kurachi, K., et al. 1985. Biochemistry24, 5494.
This antibody has been selected for its ability to neutralize the biological activity of human recombinant angiogenin. The activity of human recombinant angiogenin was measured based upon its ribonucleolytic activity toward yeast tRNA. Using the assay conditions described, 1 µg human recombinant angiogenin produces an absorbance change at 260 nm of ~2.0-3.0. The suggested antibody neutralization concentration required to yield 50% of the activity due to 1 µg of human recombinant angiogenin is approximately 100-150 µg of the antibody. The detection limit for human recombinant angiogenin by immunoblotting is ~5 ng/lane under reducing and non-reducing conditions. The detection limit for human recombinant angiogenin by ELISA is ~0.3 ng/well. This antibody exhibits no cross-reactivity with other cytokines when tested in ELISA. Antibody should be titrated for optimal results in individual systems.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
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Alexandra Skorupa et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 32(15), 5024-5038 (2012-04-13)
Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disorder affecting motoneurons. Mutations in angiogenin, encoding a member of the pancreatic RNase A superfamily, segregate with ALS. We previously demonstrated that angiogenin administration shows promise as a neuroprotective therapeutic in studies
Florian Pichot et al.
Computational and structural biotechnology journal, 21, 401-417 (2023-01-10)
Modification of tRNA is an integral part of the epitranscriptome with a particularly pronounced potential to generate diversity in RNA expression. Eukaryotic tRNA contains modifications in up to 20% of their nucleotides, but not all sites are always fully modified.
Marion C Hogg et al.
Brain communications, 2(2), fcaa138-fcaa138 (2021-02-06)
Loss-of-function mutations in the ribonuclease angiogenin are associated with amyotrophic lateral sclerosis. Angiogenin has been shown to cleave transfer RNAs during stress to produce 'transfer-derived stress-induced RNAs'. Stress-induced tRNA cleavage is preserved from single-celled organisms to humans indicating it represents
Nikoletta A Gkatza et al.
PLoS biology, 17(6), e3000297-e3000297 (2019-06-15)
Posttranscriptional modifications in transfer RNA (tRNA) are often critical for normal development because they adapt protein synthesis rates to a dynamically changing microenvironment. However, the precise cellular mechanisms linking the extrinsic stimulus to the intrinsic RNA modification pathways remain largely
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