- ￥5600
- GeneTex
- 美国
- GTX31664
- 2025年08月03日
- WB, ICC/IF, ELISA
- Rabbit
- Human
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- 详细信息
- 文献和实验
- 技术资料
- 免疫原：
NOD2 antibody was raised against a synthetic peptide corresponding to 16 amino acids at the amino terminus of human NOD2.The immunogen is located within the first 50 amino acids of NOD2.
- 亚型：
IgG
- 形态：
Liquid
- 保存条件：
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
- 克隆性：
Polyclonal
- 标记物：
Unconjugated
- 适应物种：
Human
- 保质期：
12 months from the shipping date of the product.
- 抗原来源：
Human
- 目录编号：
GTX31664
- 级别：
Primary Antibodies
- 库存：
Available
- 供应商：
GeneTex
- 宿主：
Rabbit
- 应用范围：
WB, ICC/IF, ELISA
- 浓度：
1 mg/ml (Please refer to the vial label for the specific concentration.)
- 靶点：
At least four isoforms of NOD2 are known to exist; this antibody will only detect the longest isoform. NOD2 has no cross-reaction with NOD1.
- 抗体英文名：
NOD2 antibody
- 抗体名：
NOD2 抗体
- 规格：
100 μg
WB analysis of human lymph node tissue lysate using GTX31664 NOD2 antibody.
Working concentration : (A) 1 and (B) 2 μg/ml
ICC/IF analysis of Jurkat cells using GTX31664 NOD2 antibody.
Working concentration : 5 μg/ml
ICC/IF analysis of Jurkat cells using GTX31664 NOD2 antibody.
Working concentration : 20 μg/ml
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文献和实验Polymorphisms Within Epithelial Receptors: NOD2/CARD15
) within the intracytoplasmatic receptor NOD2/CARD15, which recognizes the bacterial cell wall compound muramyl-dipeptide and induces nuclear factor-KB-mediated inflammation. By performing TaqMan PCR of the three major SNPs also identified as risk factors in Crohn’s disease
Cell-Based Reporter Assay to Analyze Activation of Nod1 and Nod2
Nod1 and Nod2 are pattern recognition receptors of the mammalian innate immune system. They respond to bacterial peptidoglycan fragments and are implicated in host defense against a variety of �different bacterial pathogens. Recent studies
Generation of Antibody Molecules Through Antibody Engineering
been overcome to a large extent using genetic-engineering techniques to produce chimeric mouse/human and completely human antibodies. Such an approach is particularly suitable because of the domain structure of the antibody molecule ( 2 ), where functional
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