- ￥5600
- GeneTex
- 美国
- GTX31656
- 2025年07月15日
- WB, IHC-P, ELISA
- Rabbit
- Human
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- 详细信息
- 文献和实验
- 技术资料
- 免疫原：
DC-SIGN antibody was raised against a synthetic peptide corresponding to 21 amino acids near the center of human DC-DIGN.The immunogen is located within the last 50 amino acids of DC-SIGN.
- 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：
GTX31656
- 级别：
Primary Antibodies
- 库存：
Available
- 供应商：
GeneTex
- 宿主：
Rabbit
- 应用范围：
WB, IHC-P, ELISA
- 浓度：
1 mg/ml (Please refer to the vial label for the specific concentration.)
- 靶点：
DC-SIGN
- 抗体英文名：
DC-SIGN antibody
- 抗体名：
DC-SIGN 抗体
- 规格：
100 μg
IHC-P analysis of human lymph node tissue using GTX31656 DC-SIGN antibody.
Working concentration : 20 μg/ml
IHC-P analysis of human lymph node tissue using GTX31656 DC-SIGN antibody.
Working concentration : 10 μg/ml
WB analysis of human small intestine tissue lysate using GTX31656 DC-SIGN antibody.
Working concentration : (A) 1 and (B) 2 μg/ml
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文献和实验Determination of DC-SIGN and DC-SIGNR Repeat Region Variations
DC-SIGN and DC-SIGNR efficiently bind HIV-1 and other viral as well as nonviral pathogens and assist either cis or trans infection. Both are type II transmembrane proteins that consist of an N-terminal cytoplasmic domain, a repeat region
The C Type Lectins DC-SIGN and L-SIGN: Receptors for Viral Glycoproteins
DC-SIGN and L-SIGN are C-type lectins that recognize carbohydrate structures present on viral glycoproteins and function as attachment factors for several enveloped viruses. DC-SIGN and L-SIGN enhance viral entry and facilitate infection
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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