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- 详细信息
- 文献和实验
- 技术资料
- 免疫原:
Carrier-protein conjugated synthetic peptide encompassing a sequence within the center region of human VIP. The exact sequence is proprietary.
- 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, Rat
- 保质期:
12 months from the shipping date of the product.
- 抗原来源:
Human
- 目录编号:
GTX129997
- 级别:
Primary Antibodies
- 库存:
Available
- 供应商:
GeneTex
- 宿主:
Rabbit
- 应用范围:
WB, ICC/IF
- 浓度:
1.07 mg/ml (Please refer to the vial label for the specific concentration.)
- 靶点:
VIP
- 抗体英文名:
VIP antibody
- 抗体名:
VIP 抗体
- 规格:
100 μl/25 μl
| 规格: | 100 μl | 产品价格: | ¥4000.0 |
|---|---|---|---|
| 规格: | 25 μl | 产品价格: | ¥1700.0 |
VIP antibody detects VIP protein by immunofluorescent analysis.
Sample: DIV10 rat E18 primary cortical neuron cells were fixed in 4% PFA at RT for 15 min.
Green: VIP stained by VIP antibody (GTX129997) diluted at 1:500.
Red: beta Tubulin 3/ Tuj1, stained by beta Tubulin 3/ Tuj1 antibody [GT11710] (GTX631836) diluted at 1:500.
Blue: Fluoroshield with DAPI (GTX30920).
VIP antibody detects VIP protein by western blot analysis. Whole cell extracts (30 μg) was separated by 15% SDS-PAGE, and the membrane was blotted with VIP antibody (GTX129997) diluted at 1:1000.
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文献和实验Assay of Radiolabeled VIP Binding and Hydrolysis by Antibodies
and resolved peaks characterized by protein chemistry methods. We describe here methods for preparation and purification of vasoactive intestinal (VIP) labeled at Tyr10 with 125 I, and the use of (Tyr10_125 I)VIP to characterize antibody binding and enzymatic
相关专题 细胞凋亡专题 Vasoactive intestinal peptide (VIP) and the structurally related pituitary adenylate cyclase-activating polypeptide (PACAP), two neuropeptides present in the lymphoid microenvironment, elicit
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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