SAB3700878
Anti-Rabbit IgG (H+L), highly cross adsorbed-Peroxidase antibody produced in goat
affinity isolated antibody, lyophilized powder
别名:
HRP
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关于此项目
NACRES:
NA.46
UNSPSC Code:
12352203
Conjugate:
peroxidase conjugate
Clone:
polyclonal
Application:
immunohistochemistry
indirect ELISA
western blot
indirect ELISA
western blot
Species reactivity:
rabbit
Citations:
9
Technique(s):
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
indirect ELISA: suitable
western blot: suitable
产品名称
Anti-Rabbit IgG (H+L), highly cross adsorbed-Peroxidase antibody produced in goat, affinity isolated antibody, lyophilized powder
biological source
goat
conjugate
peroxidase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
rabbit
technique(s)
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
Quality Level
Biochem/physiol Actions
This product was prepared from monospecific antiserum by immunoaffinity chromatography using Rabbit IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Goat Serum, Rabbit IgG and Rabbit Serum. No reaction was observed against or Bovine, Chicken, Goat, Guinea Pig, Hamster, Horse, Human, Mouse, Rat and Sheep Serum Proteins.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Antibody format: IgG
Immunogen
Rabbit IgG whole molecule
Physical form
Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free
Preparation Note
Reconstitute with 1.0 mL deionized water (or equivalent).
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Lionel Gissot et al.
Biotechnology journal, 19(2), e2300512-e2300512 (2023-11-21)
Plants are gaining traction as a cost-effective and scalable platform for producing recombinant proteins. However, expressing integral membrane proteins in plants is challenging due to their hydrophobic nature. In our study, we used transient and stable expression systems in Nicotiana
Anna Georges et al.
Scientific reports, 8(1), 15833-15833 (2018-10-28)
The ubiquitin specific protease, USP7, regulates multiple cellular pathways relevant for cancer through its ability to bind and sometimes stabilize specific target proteins through deubiquitylation. To gain a more complete profile of USP7 interactions in cancer cells, we performed affinity
Gabriel O Rodríguez-Vázquez et al.
Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 166, 115352-115352 (2023-08-27)
Drug synergy allows reduced dosing, side effects and tolerance. Optimization of drug synergy chemotherapy is fundamental in acute lymphocytic leukemia and other cancers. This study aimed to analyze the pharmacodynamic synergy between the anti-metabolite cytarabine and WEE1 inhibitor adavosertib on
Anna Georges et al.
Scientific reports, 9(1), 2724-2724 (2019-02-26)
The ubiquitin specific protease 7 (USP7 or HAUSP) is known to regulate a variety of cellular processes by binding and deubiquitylating specific target proteins. To gain a more comprehensive understanding of its interactions and functions, we used affinity purification coupled
Hu-Nan Sun et al.
Molecular medicine reports, 13(6), 4927-4933 (2016-04-16)
It has previously been reported that 16α, 17α-epoxypregnenolone-20-oxime (EPREGO) exerts an inhibitory effect on nitric oxide (NO) production and inducible NO synthase (iNOS) expression in microglia. The present study aimed to investigate the effects of EPREGO on the lipopolysaccharide (LPS)‑induced
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