SAB3701084
Anti-Mouse IgG (H+L), highly cross adsorbed-Peroxidase antibody produced in rabbit
affinity isolated antibody, lyophilized powder
Synonym(s):
HRP
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.46
Recommended Products
biological source
rabbit
conjugate
peroxidase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
mouse
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 Mouse 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-Rabbit Serum, Mouse IgG, and Mouse Serum. No reaction was observed against Human Serum Proteins. Specificity was confirmed by ELISA at less than 1% cross reactivity against other Mouse or Human heavy or light chain isotypes.
Immunogen
Mouse IgG whole molecule
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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Rebecca San Gil et al.
Scientific reports, 7(1), 2387-2387 (2017-05-26)
Heat shock proteins (Hsps) are molecular chaperones that prevent the aggregation of client proteins by facilitating their refolding, or trafficking them for degradation. The chaperone activities of Hsps are dependent on dynamic protein-protein interactions, including their oligomerisation into large multi-subunit
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