추천 제품
일반 설명
IgGs are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins. Goat Anti-Rabbit IgG (whole molecule)-Alkaline Phosphatase antibody binds to all rabbit Igs.
Immunoglobulin G (IgG) is part of the immunoglobulin family and is widely expressed in the serum. It consists of a gamma (γ) heavy chain in the constant (C) region. The monomeric structure of IgG consists of two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity (Fab fragments). The third fragment known as fragment crystallizable (Fc).
면역원
purified rabbit IgG
애플리케이션
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)
Western Blotting (1 paper)
Enzyme-linked immunosorbent assay (1 paper)
Western Blotting (1 paper)
Citrullination of antithrombin by PADI4 was analyzed by ELISA using alkaline phosphatase conjugated goat anti-rabbit IgG as the secondary diluted at 1:5000 in 0.05M carbonate/bicarbonate buffer (Ph 9.6).
Goat Anti-Rabbit IgG (whole molecule)-Alkaline Phosphatase antibody has been used for ELISA assays at a dilution of 1:5,000.
Protein expression in maize endosperm amyloplast preparations or whole cell lysates were analyzed by alkaline phosphatase-conjugated goat anti-rabbit IgG as the secondary antibody.
물리적 형태
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 50% glycerol, and 15 mM sodium azide.
면책조항
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
S Zucchelli et al.
Journal of virology, 74(24), 11598-11607 (2000-11-23)
We describe an improved genetic immunization strategy for eliciting a full spectrum of anti-hepatitis C virus (HCV) envelope 2 (E2) glycoprotein responses in mammals through electrical gene transfer (EGT) of plasmid DNA into muscle fibers. Intramuscular injection of a plasmid
M C de Beer et al.
The Biochemical journal, 283 ( Pt 3), 673-678 (1992-05-01)
Four serum amyloid A protein (SAA) genes and two gene products, apo-SAA1 and apo-SAA2 were identified in BALB/c mice (type A). SJL/J mice (type B) are thought to be defective in apo-SAA2 expression. A unique variant of mouse apo-SAA was
F Trevisan et al.
Plant disease, 90(8), 1026-1030 (2006-08-01)
We report the use of the coat protein (CP) gene from Passion fruit woodiness virus (PWV) to produce resistant transgenic plants of yellow passion fruit. A full-length CP gene from a severe PWV isolate from the state of São Paulo
Jens Madsen et al.
PloS one, 8(5), e64441-e64441 (2013-05-22)
The protein deleted in malignant brain tumors (DMBT1) and the trefoil factor (TFF) proteins have all been proposed to have roles in epithelial cell growth and cell differentiation and shown to be up regulated in inflammatory bowel diseases. A panel
J Keener et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(25), 13458-13462 (1998-02-12)
RNA polymerase I (Pol I) transcription in the yeast Saccharomyces cerevisiae is greatly stimulated in vivo and in vitro by the multiprotein complex, upstream activation factor (UAF). UAF binds tightly to the upstream element of the rDNA promoter, such that
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