SAB3700863
Anti-Rabbit IgG (Fc specific)-Peroxidase antibody produced in donkey
affinity isolated antibody, lyophilized powder
Synonym(s):
HRP
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About This Item
Recommended Products
biological source
donkey
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
Specificity
This product was prepared from monospecific antiserum by immunoaffinity chromatography using Rabbit IgG coupled to agarose beads. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Donkey Serum, Rabbit IgG, Rabbit IgG F(c) and Rabbit Serum. No reaction was observed against Rabbit IgG F(ab′)2
Immunogen
Rabbit IgG F(c) fragment
Physical properties
Antibody format: IgG
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
Reconstitution
Reconstitute with 1.0 mL deionized water (or equivalent).
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.
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Certificates of Analysis (COA)
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Oncology letters, 16(5), 6059-6064 (2018-10-23)
The aquaporin (AQP) family, which includes 13 members identified in mammalian cells, is involved in cancer development and progression. AQP9 expression is upregulated in several tumor tissue types. However, the functions of AQP9 in astrocytoma remain elusive. The present study
International journal of molecular sciences, 24(22) (2023-11-25)
Balancing peptidoglycan (PG) synthesis and degradation with precision is essential for bacterial growth, yet our comprehension of this intricate process remains limited. The NlpI-Prc proteolytic complex plays a crucial but poorly understood role in the regulation of multiple enzymes involved
eLife, 9 (2020-08-22)
Membrane proteins with multiple transmembrane domains play critical roles in cell physiology, but little is known about the machinery coordinating their biogenesis at the endoplasmic reticulum. Here we describe a ~ 360 kDa ribosome-associated complex comprising the core Sec61 channel
Nature, 611(7934), 167-172 (2022-10-20)
Most membrane proteins are synthesized on endoplasmic reticulum (ER)-bound ribosomes docked at the translocon, a heterogeneous ensemble of transmembrane factors operating on the nascent chain1,2. How the translocon coordinates the actions of these factors to accommodate its different substrates is
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