Sonic Hedgehog anticorps (N-Term)

N° du produit ABIN5540856

L’anticorps Rat Monoclonal anti-Sonic Hedgehog a été validé pour WB, IHC (fro) et Neut. Il convient pour détecter Sonic Hedgehog dans des échantillons de Souris.

Aperçu rapide pour Sonic Hedgehog anticorps (N-Term) (ABIN5540856)

Antigène: Sonic Hedgehog (SHH)

Reactivité: Souris

Hôte: Rat

Clonalité: Monoclonal

Conjugué: Cet anticorp Sonic Hedgehog est non-conjugé

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

Clone: 6K12

Détail du produit anti-Sonic Hedgehog anticorps

Épitope: N-Term

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

Purification: Affinity Chromatography on Protein A/G

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

Isotype: IgG2

Information d'application

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

Restrictions: For Research Use only

Stockage

Buffer: Purification: Affinity Chromatography on Protein A/G

Stock: 4 °C,-20 °C

Stockage commentaire: 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.

Date de péremption: 12 months

Détails sur Sonic Hedgehog

Antigène: Sonic Hedgehog (SHH)

Sujet: 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: Signalisation Hedgehog, Dopaminergic Neurogenesis, Regulation of Muscle Cell Differentiation, Tube Formation, Skeletal Muscle Fiber Development