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Sonic Hedgehog 抗体 (N-Term)

This anti-Sonic Hedgehog antibody is a 大鼠 单克隆 antibody detecting Sonic Hedgehog in WB, IHC (fro) 和 Neut. Suitable for 小鼠.
产品编号 ABIN5540856
发货至: 中国

Quick Overview for Sonic Hedgehog 抗体 (N-Term) (ABIN5540856)

抗原

See all Sonic Hedgehog (SHH) 抗体
Sonic Hedgehog (SHH)

适用

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小鼠

宿主

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  • 8
  • 1
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大鼠

克隆类型

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  • 40
单克隆

标记

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This Sonic Hedgehog antibody is un-conjugated

应用范围

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Western Blotting (WB), Immunohistochemistry (Frozen Sections) (IHC (fro)), Neutralization (Neut)

克隆位点

6K12
  • 抗原表位

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    N-Term

    特异性

    This antibody detects Mouse Shh with Western Blot. Species: Mouse.

    纯化方法

    Affinity Chromatography on Protein A/G

    免疫原

    Recombinant Mouse Sonic Hedgehog (Shh) N-Terminal fragment.

    亚型

    IgG2
  • 应用备注

    Western Blot: 1/250-1/1000. Neutralization. Immunohistochemistry on Frozen Sections: 1/50-1/200.

    限制

    仅限研究用
  • 缓冲液

    Purification: Affinity Chromatography on Protein A/G

    储存条件

    4 °C,-20 °C

    储存方法

    Store lyophilized at 2-8°C for 6 months or at -20°C long term. After reconstitution store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C long term. Avoid repeated freezing and thawing. Shelf life: one year from despatch.

    有效期

    12 months
  • 抗原

    Sonic Hedgehog (SHH)

    背景

    Human Shh cDNA encodes a 462 amino acid (aa) residue (45 kDa) precursor protein with a 23 aa signal peptide. An autocatalytic cleavage reaction yields a 19 kDa (residues 24 - 197) amino-terminal fragment (Shh-N), and a 25 kDa (residues 198 - 462) carboxy-terminal domain (Shh-C). The N-terminal domain retains all known signaling capabilities, while the C-terminal domain is responsible for the intramolecular processing, acting as a cholesterol transferase that covalently transfers the cholesterol molecule to the C-terminus of Shh-N. When Shh is expressed in insect or mammalian cells, a palmitoyl group is also attached to the N-terminal cysteine of Shh-N via an amide linkage. Although the binding affinity to their receptors is not changed, lipid-modified Shh-N proteins are more potent than the unmodified proteins in cell-based assays. Other hydrophobic modifications to unmodified Shh-N, including the substitution of the N-terminal cysteine residue with two hydrophobic isoleucine residues, can also increase Shh-N potency.

    UniProt

    Q62226

    途径

    Hedgehog Signaling, Dopaminergic Neurogenesis, Regulation of Muscle Cell Differentiation, Tube Formation, Skeletal Muscle Fiber Development
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