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iNOS Antibody

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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年11月20日
  • W
  • Rabbit
  • M,H
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    • 详细信息
    • 询价记录
    • 文献和实验
    • 技术资料
    • 抗体英文名

      iNOS Antibody

    • 抗原

      synthetic peptide surrounding Ser1000 of human iNOS

    • 应用范围

      W

    • 宿主

      Rabbit

    • 库存

      大量

    • 保质期

      详见说明书

    • 供应商

      CST

    • 适应物种

      M,H

    • 级别

      详见MSDS文件

    • 是否单克隆

      2

    • 保存条件

      -20°c

    • 规格

      100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting
    Reactivity Key:  H=Human  M=Mouse
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W M (H) Endogenous 130 Rabbit
    Protocols
    Specificity / Sensitivity

    iNOS Antibody detects endogenous levels of total iNOS protein.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide surrounding Ser1000 of human iNOS. Antibodies are purified by protein A and peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from Raw264.7 cells, untreated or LPS-treated (1 µg/ml for 6 h), using iNOS Antibody.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from Raw264.7 cells, untreated or LPS-treated (1 μg/ml for 6 h), using iNOS Antibody.

    Background

    Nitric Oxide Synthase (NOS) catalyses the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

    Nitric oxide produced by iNOS is involved in host defense against protozoa, bacteria, fungi and viruses. Unlike constitutively expressed eNOS and nNos, iNOS is not usually expressed in quiescent cells. iNOS is transcriptionally induced in response to bacterial endotoxins such as LPS and proinflammatory cytokines in macrophages and various other cell types. Transcription factors involved in iNOS transcription include NF-κB, AP-1 and STAT. Different signaling pathways either promote (Jak1/2, PKC, c-Raf, p38 MAP kinase and p44/42 MAP kinase) or inhibit (PI3 kinase) iNOS expression depending on stimulus and cell type (4).

    1. Tsutsui, M. (2004) J Atheroscler Thromb 11, 41-48.
    2. Son, H. et al. (1996) Cell 87, 1015-10123.
    3. Hawkins, R.D. (1996) Neuron 16, 465-467.
    4. Bogdan, C. (2001) Nat Immunol 2, 907-16.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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    相关实验
    • 犬诱导型一氧化合成酶(iNOS)酶联免疫分析(ELISA)

      犬 诱导型一氧化合成酶(iNOS ) 酶联免疫分析(ELISA ) 试剂盒使用说明书 本试剂仅供研究使用         目的:本试剂盒用于测定犬血清,血浆及相关液体样本中 诱导型一氧化合成酶(iNOS ) 的 含量。 实验原理: 本试剂盒应用双抗体夹心法测定标本中 犬 诱导型一氧化合成酶( iNOS ) 水平。用纯化的 犬 诱导型一氧化合成酶( iNOS ) 抗体包被微孔板,制成固相抗体,往包被单抗的微孔中依次加入 诱导型一氧

    • Cell Protection by Inhibition of iNOS Through Lentiviral Vector-Based Strategies

      toxicity. We identified that NF-κB-dependent induction of iNOS is a critical determinant of β cell fate following cytokine exposure. Having identified the pivotal role of iNOS activation in cytokine-induced β cell pathophysiology, lentiviral vectors

    • 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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