Human IHH protein (Recombinant) (N-His) (STJP005406)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human IHH-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | IHH |
| Gene ID | 3549 |
| Uniprot ID | IHH_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Phe240-Gly399 |
Additional Info
| Post Translational Modifications | Indian hedgehog protein N-product: Cholesterylation is required for N-product targeting to lipid rafts and multimerization. Indian hedgehog protein: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product. The N-product is the active species in both local and long-range signaling, whereas the C-product is degraded in the endoplasmic reticulum. Indian hedgehog protein N-product: N-palmitoylation by HHAT of N-product is required for indian hedgehog protein N-product multimerization and full activity. |
| Function | Plays a role in embryonic morphogenesis.it is involved in the regulation of endochondral skeleton formation, and the development of retinal pigment epithelium (RPE), photoreceptors and periocular tissues. Indian hedgehog protein: The C-terminal part of the indian hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein into two parts followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product. Both activities occur in the endoplasmic reticulum. Plays a role in hedgehog paracrine signaling. Associated with the very-low-density lipoprotein (VLDL) particles to function as a circulating morphogen for endothelial cell integrity maintenance. Indian hedgehog protein N-product: The dually lipidated indian hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development. Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. Plays a role in morphogenesis of the skeleton by coordinating growth and differentiation of the endochondral skeleton. Positively regulates PTHLH expression during endochondral bone formation preventing chondrocyte hypertrophy. In contrast, participates in normal chondrocyte proliferation in a PTHLH-independent pathway. |
| Protein Name | Indian Hedgehog ProteinIhhHhg-2 Cleaved Into - Indian Hedgehog Protein N-Product |
| Database Links | Reactome: R-HSA-373080Reactome: R-HSA-5358346Reactome: R-HSA-5362798Reactome: R-HSA-5632681Reactome: R-HSA-5632684Reactome: R-HSA-5635838Reactome: R-HSA-5658034Reactome: R-HSA-8941284Reactome: R-HSA-9758920 |
| Cellular Localisation | Indian Hedgehog Protein N-Product: Cell MembraneLipid-AnchorThe N-Product Remains Associated With The Cell SurfaceIndian Hedgehog Protein: Endoplasmic Reticulum MembraneGolgi Apparatus MembraneSecretedCo-Localizes With Hhat In The Er And Golgi Membrane |
| Alternative Protein Names | Indian Hedgehog Protein proteinIhh proteinHhg-2 Cleaved Into - Indian Hedgehog Protein N-Product proteinIHH protein |
Information sourced from Uniprot.org