- ￥5600
- GeneTex
- 美国
- GTX27505
- 2025年07月12日
- IHC-P, IHC
- Mouse
- Human, Mouse
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- 详细信息
- 文献和实验
- 技术资料
- 免疫原：
Human amyloid A protein coupled to horseradish peroxidase and kininogen.
- 亚型：
IgG2a
- 形态：
Liquid
- 保存条件：
Store as concentrated solution. Centrifuge briefly prior to opening vial. Store at 4ºC.
- 克隆性：
Monoclonal
- 标记物：
Unconjugated
- 适应物种：
Human, Mouse
- 保质期：
12 months from the shipping date of the product.
- 抗原来源：
Human
- 目录编号：
GTX27505
- 级别：
Primary Antibodies
- 库存：
Available
- 供应商：
GeneTex
- 宿主：
Mouse
- 应用范围：
IHC-P, IHC
- 浓度：
Batch dependent (Please refer to the vial label for the specific concentration.)
- 靶点：
This antibody reacts with amyloid deposits in all organs and tissues. It reacts specifically with amyloid A protein in the native fibrils as well as fixed fibrils but does not show any reactivity with non-amyloid A fibril protein.
- 抗体英文名：
Amyloid A Component antibody [mcl] (ready-to-use)
- 抗体名：
Amyloid A Component 抗体 [mcl] (ready-to-use)
- 规格：
6 ml
IHC-P analysis of human kidney tissue using GTX27505 Amyloid A Component antibody [mcl] (ready-to-use).
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文献和实验Levine S et al., Exp Mol Pathol 2009 (PMID:19041304)
Expression of VHH Antibody Fragments in Saccharomyces cerevisiae
The use of Saccharomyces cerevisiae as a production host for heterologous proteins has several advantages compared to the use of a bacterial host. First, S. cerevisiae has proven to be a productive host capable of expressing many heterologous
Preparation of Immunoconjugates Using Antibody Oligosaccharide Moieties
or loss of the antigen binding function, resulting in a defective antibody conjugate that lacks one of its component functions. Furthermore, even if the chemical derivatization does not affect the antigen binding function, the subsequent coupling
Preparation of Recombinant Viral Glycoproteins for Novel and Therapeutic Antibody Discovery
of virus neutralization, and in the eventual development of specific entry inhibitors, vaccines, and research tools. The majority of the more recently developed antiviral hmAbs have come from the use of antibody phage-display technologies using both na�ve
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