抗HGF Receptor抗体(Anti-HGF Receptor, c-Met, Human, Goat-Poly, Biotin antibody)
掲載日情報:2021/01/28 現在Webページ番号:27604
HGF Receptorに対する抗体(Anti-HGF Receptor, c-Met, Human, Goat-Poly, Biotin )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。
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- 価格
- Product Details
- Applications and Data
- Data Examples
- References
- Related Research Areas
- Related Product & Information
- Citations
価格
[在庫・価格 :2024年05月18日 00時00分現在]
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Anti-HGF Receptor, c-Met, Human, Goat-Poly, Biotin |
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[在庫・価格 :2024年05月18日 00時00分現在]
Anti-HGF Receptor, c-Met, Human, Goat-Poly, Biotin
文献数: 9
- 商品コード:BAF358
- メーカー:RSD
- 包装:50μg
- 価格:¥120,000
- 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 |
マッチドペア:Human HGF R/c-MET サンドイッチELISAの検出用抗体として利用可能,補足用抗体として#MAB3581-500,スタンダードとして#358-MT-100を用いる。 別名:AUTS9 Genbank No: 4233 Protein Accession No: P08581 |
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法規制等 | |||
保存条件 | -20℃ | 法規備考 | |
抗原種 | Human | 免疫動物 | Goat |
交差性 | Human | 適用 | ELISA,FCM,Western Blot |
標識 | Biotin | 性状 | Antigen Affinity Purified |
吸収処理 | クラス | IgG | |
クロナリティ | Polyclonal | フォーマット | |
掲載カタログ |
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製品記事 | |||
関連記事 |
R&D Systems(R&Dシステムズ)社 ELISA用ペア抗体を使用したELISA 構築ガイド |
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Product Details
Species Reactivity | Human |
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Label | Biotin |
Immunogen | Mouse myeloma cell line NS0-derived recombinant human HGF R/c-METGlu25-Thr932Accession # P08581 |
Source | Polyclonal Goat IgG |
Purification | Antigen Affinity-purified |
Specificity | Detects human HGF R/c-MET in ELISAs and Western blots. In Western blot, this antibody shows approximately 50% cross-reactivity with recombinant mouse HGF R. |
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Applications and Data
Recommended Concentration | Sample | |
Western Blot | 0.1 µg/mL | Recombinant Human HGF R/c-MET Fc Chimera (Catalog # 358-MT) |
Flow Cytometry | 2.5 µg/106 cells | See below |
Human HGF R/c-MET Sandwich Immunoassay | Reagent | |
ELISA Capture (Matched Antibody Pair) | 2-8 µg/mL | Human HGF R/c‑MET Antibody (Catalog #MAB3581 ) |
ELISA Detection (Matched Antibody Pair) | 0.1-0.4 µg/mL | Human HGF R/c‑MET Biotinylated Antibody (Catalog #BAF358 ) |
ELISA Standard | Recombinant Human HGF R/c-MET Fc Chimera His-tag Protein (Catalog #358-MT ) | |
Please Note: Optimal dilutions should be determined by each laboratory for each application.General Protocolsare available in the Technical Information section on our website. |
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Data Examples
Flow Cytometry |
click image to view larger | Detection of HGF R/c‑MET in MDA‑MB‑231 Human Cell Line by Flow Cytometry.MDA‑MB‑231 human breast cancer cell line was stained with Human HGF R/c‑MET Biotinylated Antigen Affinity‑purified Polyclonal Antibody (Catalog # BAF358, filled histogram) or control antibody (Catalog # BAF108, open histogram), followed by Streptavidin-Allophycocyanin (Catalog # F0050). |
Reconstitution | Reconstitute at 0.2 mg/mL in sterile PBS. | Reconstitution Buffer Available |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | |
Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. | |
1 month, 2 to 8 °C under sterile conditions after reconstitution. | ||
6 months, -20 to -70 °C under sterile conditions after reconstitution. | ||
Background: HGF R/c-MET | HGF R, also known as Met (from N-methyl-N’-nitro-N-nitrosoguanidine induced), is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. This generates a mature HGF R that is a disulfide-linked dimer composed of a 50 kDa extracellular alpha chain and a 145 kDa transmembrane beta chain (1, 2). The extracellular domain (ECD) contains a seven bladed beta -propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain (3, 4). Proteolysis and alternate splicing generate additional forms of human HGF R which either lack the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the alpha and beta chains (5-7). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 8). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (9, 10). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (11). In the absence of ligand, HGF R forms noncovalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, Integrin alpha 6/ beta 4, Plexins B1, 2, 3, and MSP R/Ron (12-19). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (12-19). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (12, 16, 17). Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells (20). Genetic polymorphisms, chromosomal translocation, overexpression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, human HGF R shares 86-88% aa sequence identity with canine, mouse, and rat HGF R. |
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References
Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915. | |
Corso, S. et al. (2005) Trends Mol. Med. 11:284. | |
Gherardi, E. et al. (2003) Proc. Natl. Acad. Sci. USA 100:12039. | |
Park, M. et al. (1987) Proc. Natl. Acad. Sci. USA 84:6379. | |
Crepaldi, T. et al. (1994) J. Biol. Chem. 269:1750. | |
Prat, M. et al. (1991) Mol. Cell. Biol. 12:5954. | |
Rodrigues, G.A. et al. (1991) Mol. Cell. Biol. 11:2962. | |
Kong-Beltran, M. et al. (2004) Cancer Cell 6:75. | |
Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793. | |
Ponzetto, C. et al. (1994) Cell 77:261. | |
Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799. | |
Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074. | |
Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408. | |
Jo, M. et al. (2000) J. Biol. Chem. 275:8806. | |
Wang, X. et al. (2002) Mol. Cell 9:411. | |
Trusolino, L. et al. (2001) Cell 107:643. | |
Giordano, S. et al. (2002) Nat. Cell Biol. 4:720. | |
Conrotto, P. et al. (2004) Oncogene 23:5131. | |
Follenzi, A. et al. (2000) Oncogene 19:3041. | |
Sonnenberg, E. et al. (1993) J. Cell Biol. 123:223. | |
Long Name: | Hepatocyte Growth Factor Receptor |
Entrez Gene IDs: | 4233 (Human); 17295 (Mouse) |
Alternate Names: | AUTS9; cMET; c-MET; EC 2.7.10; EC 2.7.10.1; hepatocyte growth factor receptor; HGF R; HGF receptor; HGF/SF receptor; HGFR; Met (c-Met); met proto-oncogene (hepatocyte growth factor receptor); met proto-oncogene tyrosine kinase; MET; oncogene MET; Proto-oncogene c-Met; RCCP2; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met |
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Related Research Areas
Cancer Biomarkers | ||
Cancer Stem Cell Markers | ||
Cytokine and Growth Factor Receptors on VSMC | ||
Cytokines and Receptors in Angiogenesis | ||
Hepatic Endoderm | ||
Hepatic Endoderm Cell Markers | ||
HIF Transcription Factors | ||
Receptor Tyrosine Kinases (RTKs) | ||
Receptor Tyrosine Kinases (RTKs) in the Akt Pathway | ||
Receptors in the Jak/STAT Pathway | ||
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Related Product & Information
Background | HGF R/c-MET |
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background_content | Background: HGF R/c-MET HGF R, also known as Met (from N-methyl-N’-nitro-N-nitrosoguanidine induced), is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. This generates a mature HGF R that is a disulfide-linked dimer composed of a 50 kDa extracellular alpha chain and a 145 kDa transmembrane beta chain (1, 2). The extracellular domain (ECD) contains a seven bladed beta -propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain (3, 4). Proteolysis and alternate splicing generate additional forms of human HGF R which either lack the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the alpha and beta chains (5-7). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 8). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (9, 10). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (11). In the absence of ligand, HGF R forms noncovalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, Integrin alpha 6/ beta 4, Plexins B1, 2, 3, and MSP R/Ron (12-19). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (12-19). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (12, 16, 17). Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells (20). Genetic polymorphisms, chromosomal translocation, overexpression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, human HGF R shares 86-88% aa sequence identity with canine, mouse, and rat HGF R. |
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Citations
- Tumor and Plasma Met Levels in Non-Metastatic Prostate Cancer
Authors: Deborah R Kaye
PLoS ONE, 2016;11(6):e0157130.
Species: Human
Sample Type: Whole Tissue
Application: ELISA Capture - A pharmacodynamic/pharmacokinetic study of ficlatuzumab in patients with advanced solid tumors and liver metastases.
Authors: Tabernero J, Elez M, Herranz M, Rico I, Prudkin L, Andreu J, Mateos J, Carreras M, Han M, Gifford J, Credi M, Yin W, Agarwal S, Komarnitsky P, Baselga J
Clin Cancer Res, 2014;20(10):2793-804.
Species: Human
Sample Type: Serum
Application: ELISA Capture - The Pim-1 protein kinase is an important regulator of MET receptor tyrosine kinase levels and signaling.
Authors: Cen B, Xiong Y, Song J, Mahajan S, DuPont R, McEachern K, DeAngelo D, Cortes J, Minden M, Ebens A, Mims A, LaRue A, Kraft A
Mol Cell Biol, 2014;34(13):2517-32.
Species: Human
Sample Type: Cell Lysates
Application: WB - Safety, pharmacokinetics, and pharmacodynamics of AMG 102, a fully human hepatocyte growth factor-neutralizing monoclonal antibody, in a first-in-human study of patients with advanced solid tumors.
Authors: Gordon MS, Sweeney CS, Mendelson DS
Clin. Cancer Res., 2010;16(2):699-710.
Species: Human
Sample Type: Plasma
Application: Electrochemiluminescent Assay - Soluble c-Met receptors inhibit phosphorylation of c-Met and growth of hepatocyte growth factor: c-Met-dependent tumors in animal models.
Authors: Coxon A, Rex K, Meyer S, Sun J, Sun J, Chen Q, Radinsky R, Kendall R, Burgess TL
Mol. Cancer Ther., 2009;0(0):.
Species: Human
Sample Type: Cell Lysates
Application: Electrochemiluminescence
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