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MilliporeSigma

A9037

Sigma-Aldrich

Anti-Rat IgG (whole molecule)−Peroxidase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti Rat, Anti Rat Hrp

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

conjugate

peroxidase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct ELISA: 1:10,000

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Categorías relacionadas

General description

IgGs are glycoprotein antibodies that modulate several immune responses. Rat IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rat IgG conjugated to a detectable substrate is a useful tool for the analysis of target proteins. Anti-Rat IgG (whole molecule)-Peroxidase antibody binds all rat immunoglobulins.
IgG (immunoglobulin γ) is a monomeric antibody containing a γ Fc region as a part of heavy chain, which is linked to the Fab arm through a hinge region. It is the most abundant serum antibody and constitutes to 70% of the total immunoglobulins.

Immunogen

Purified rat IgG

Application

Anti-Rat IgG (whole molecule)-Peroxidase antibody is suitable for use in ELISA and immunoblot at 1:5000 dilutions.
Lysates generated from primary cells isolated from lymphoid organs of P. monodon shrimp were analyzed by western blot using HRP-conjugated goat anti-rat as the secondary antibody at a 1:4000 dilution.

Biochem/physiol Actions

IgG (immunoglobulin γ), upon epitope binding, mediates the activation of classical complement pathway. Interaction between the host cell membrane and IgG antibody results in type II hypersensitivity reaction. Decreased serum levels of IgG contributes to common variable immunodeficiency, thus making the individual easily prone to infections.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin with preservative

Preparation Note

Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, Elsevier/North Holland Biomedical Press, Amsterdam, p215 (1978).

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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Warning

Hazard Classifications

Aquatic Chronic 2 - Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Máximo Lopez Medus et al.
Scientific reports, 7(1), 8788-8788 (2017-08-20)
Nearly one third of the eukaryotic proteome traverses the secretory pathway and most of these proteins are N-glycosylated in the lumen of the endoplasmic reticulum. N-glycans fulfill multiple structural and biological functions, and are crucial for productive folding of many
Wanchai Assavalapsakul et al.
Journal of virology, 80(1), 262-269 (2005-12-15)
The yellow head virus is a positive-sense, single-stranded RNA virus that causes significant mortality in farmed penaeid shrimp. This study sought to isolate and characterize the receptor protein used by the virus to gain entry into Penaeus monodon Oka (lymphoid)
T Orth et al.
European journal of clinical investigation, 29(11), 929-939 (1999-12-03)
In sera from patients with autoimmune liver diseases, e. g. primary sclerosing cholangitis (PSC) and autoimmune hepatitis, anti-neutrophil cytoplasmic antibodies (ANCAs) can be found. Until now, no animal model of ANCA induction in liver disease has been described. In this
Trevor R F Smith et al.
Vaccine, 35(21), 2840-2847 (2017-04-18)
Respiratory syncytial virus (RSV) is a massive medical burden in infants, children and the elderly worldwide, and an effective, safe RSV vaccine remains an unmet need. Here we assess a novel vaccination strategy based on the intradermal delivery of a
Hyunsuk Suh et al.
Molecular cell, 61(2), 297-304 (2016-01-23)
Dynamic interactions between RNA polymerase II and various mRNA-processing and chromatin-modifying enzymes are mediated by the changing phosphorylation pattern on the C-terminal domain (CTD) of polymerase subunit Rpb1 during different stages of transcription. Phosphorylations within the repetitive heptamer sequence (YSPTSPS)

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