Sonic Hedgehog/Shh, N-Terminus 組換え体(リコンビナント)タンパク質 | Recombinant Human Sonic Hedgehog/Shh, N-Terminus
掲載日情報:2015/01/26 現在Webページ番号:111617
R&D Systems社製の高品質なSonic Hedgehog/Shh, N-Terminusの組換え体タンパク質(Recombinant Human Sonic Hedgehog/Shh, N-Terminus)です。
※本製品は研究用です。研究用以外には使用できません。
[在庫・価格 :2025年05月02日 20時55分現在]
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Shh, N-Terminal Peptide, Human, Recombinant, Carrier-free <Sonic Hedgehog> |
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[在庫・価格 :2025年05月02日 20時55分現在]
Shh, N-terminal Peptide, Human, Recombinant <Sonic Hedgehog>
文献数: 18
- 商品コード:1314-SH-025
- メーカー:RSD
- 包装:25μg
- 価格:¥61,000
- 在庫:無(未発注)
- 納期:10日程度 ※※ 表示されている納期は弊社に在庫がなく、取り寄せた場合の目安納期となります。
- 法規制等:
説明文 | 産生:E. coli,純度:>97%, by SDS-PAGE with silver staining, under reducing conditions,由来動物:Human,M.W.:20 kDa,Genbank:6469,エンドトキシンレベル:<0.10 EU per 1 µg of the protein by the LAL method. 別名:HHG1 Genbank No: 6469 Protein Accession No: Q15465 |
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保存条件 | -20℃ | 法規備考 | |
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製品記事 | R&D Systems社 Hedgehog Family関連製品 |
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関連記事 |
Shh, N-Terminal Peptide, Human, Recombinant, Carrier-free <Sonic Hedgehog>
文献数: 0
- 商品コード:1314-SH-025/CF
- メーカー:RSD
- 包装:25μg
- 価格:¥61,000
- 在庫:無(未発注)
- 納期:10日程度 ※※ 表示されている納期は弊社に在庫がなく、取り寄せた場合の目安納期となります。
- 法規制等:
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バルク注文に関して
※バルク包装品も承ります。お気軽にお問合せ下さい。
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CF(Carrier-Free)とは?
R&D Systems社組換え体タンパク質製品では通常ウシ血清アルブミン(BSA)をキャリアタンパク質として加えています。キャリアタンパク質を加えることで組換え体タンパク質の安定性が高まり、使用期限が長くなります。また、より濃度の低い溶液での保管も可能となります。CF製品はBSAが含まれない製品となります。一般的に細胞培養や、ELISAのスタンダードにはBSA含有製品を推奨しています。CF製品はBSAが影響してしまうアプリケーションに推奨されます。
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Product Details
- Source
- E. coli-derived, Cys24-Gly197, with a C-terminal 6-His tag
- Accession
- Q15465
- Purity
- >97%, by SDS-PAGE with silver staining, under reducing conditions.
- Predicted Molecular Mass
- 20 kDa
- SDS-PAGE
- 22 kDa, reducing conditions
- Activity
- Measured by its ability to induce alkaline phosphatase production by C3H10T1/2 mouse embryonic fibroblast cells. Nakamura, T. et al. (1997) Biochem. Biophys. Res. Commun. 237
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Additional Information
- Molecule Information
- Sonic Hedgehog/Shh
- Aliases
- Shh
- Entrez Gene IDs
- 6469 (Human); 20423 (Mouse)
- Background
- Sonic Hedgehog
- 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. At the cell surface, Shh-N activity is mediated by a multicomponent receptor complex involving the 12-pass transmembrane protein, Patched (Ptc) which binds Shh with high affinity and Smoothened (Smo), a signaling seven transmembrane G-protein coupled receptor. In the absence of Shh, Ptc represses Smo activity. The binding of Shh to Ptc releases the basal repression of Smo by Ptc. Shh is expressed in key embryonic tissues such as the Hensen’s node, the zone of polarizing activity in the posterior limb bud, the notochord, and the floor plate of the neural tube. Shh is involved in regulating the patterning of the developing central nervous system, somite, and limb. Shh plays an important role in the development of particular tissues such as whisker, hair, foregut, tooth and bone. Studies suggest that Shh is involved in regulating stem cell fates of neural and hematopoeitic lineages, and that aberrant Shh signaling is implicated in basal cell carcinomas and other diseases.
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Citations
Citations of cell biology reagents in peer reviewed literature can be used as a direct measure of product quality. They can also provide crucial insightinto their use under specialized or unique experimental conditions. Because of the importance published citations have to researchers, R&D Systems personnelmanually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but alsoprovides information about sample types, species, and experimental conditions.
Derivation of cerebellar neurons from human pluripotent stem cells.
Bhattacharya S, Erceg S, Lukovic D, Moreno-Manzano V, Stojkovic M
Curr Protoc Stem Cell Biol 2012 20:1H.51
The hedgehog system in ovarian follicles of cattle selected for twin ovulations and births: evidence of a link between the IGF and hedgehog systems.
Aad , Pauline , Echternkamp , Sherrill, Schreiber , Nicole B, Spicer , Leon J, Sypherd , David D
Biol Reprod 2012 87:79
Vitronectin promotes oligodendrocyte differentiation during neurogenesis of human embryonic stem cells.
Gil JE, Kim JH, Kim SE, Kim SK, Paek SH, Park SH, Shim JH, Woo DH, You HJ
FEBS Lett. 2009 583:561-7
Species: Human
Protein Application: Bioassay
Human ES cell-derived neural rosettes reveal a functionally distinct early neural stem cell stage.
Al Shamy G, Elkabetz Y, Panagiotakos G, Socci ND, Studer L, Tabar V
Genes Dev. 2008 22:152-65
Species: Human
Protein Application: Bioassay
Reduced pepsin A processing of sonic hedgehog in parietal cells precedes gastric atrophy and transformation.
Bai L, Dlugosz A, L Gumucio D, Merchant JL, Samuelson LC, Tessier A, Todisco A, Waghray M, Zavros Y
J. Biol. Chem. 2007 282:33265-74
Species: N/A
Protein Application: SDS-page
An early role for WNT signaling in specifying neural patterns of Cdx and Hox gene expression and motor neuron subtype identity.
Edlund T, Jessell TM, Maier E, Nordstrom U
PLoS Biol. 2006 4:e252
Species: Chicken
Protein Application: Bioassay
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