Sonic Hedgehog antibody (N-Term)

Catalog No. ABIN5540856

The Rat Monoclonal anti-Sonic Hedgehog antibody is suitable to detect Sonic Hedgehog in samples from Mouse. It has been validated for WB, IHC (fro) and Neut.

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

Target: Sonic Hedgehog (SHH)

Reactivity: Mouse

Host: Rat

Clonality: Monoclonal

Conjugate: This Sonic Hedgehog antibody is un-conjugated

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

Clone: 6K12

Product Details anti-Sonic Hedgehog Antibody

Binding Specificity: N-Term

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

Purification: Affinity Chromatography on Protein A/G

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

Isotype: IgG2

Application Details

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

Restrictions: For Research Use only

Handling

Buffer: Purification: Affinity Chromatography on Protein A/G

Storage: 4 °C,-20 °C

Storage Comment: 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.

Expiry Date: 12 months

Target Details for Sonic Hedgehog

Target: Sonic Hedgehog (SHH)

Background: 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

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