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TIMP1 Antibody

    应用:
  • WB
  • 宿主种属: 兔(Rabbit)
  • 种属反应性: 人(Human)
  • 亚型: Rabbit IgG
  • 偶联: Unconjugated
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库存信息

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库存信息

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库存信息

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库存信息

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货号 (SKU) 包装规格 是否现货 价格 数量
Ab131327-10μl
10μl 现货 Stock Image
Ab131327-50μl
50μL 现货 Stock Image
Ab131327-100μl
100μL 期货 Stock Image
Ab131327-1ml
1ml 期货 Stock Image

基本信息

产品名称 TIMP1 Antibody
别名 TIMP1抗体 | 金属蛋白酶组织抑制因子-1抗体 | TIMP1抗体
英文别名 Clgi antibody | Collagenase inhibitor antibody | Collagenase inhibitor, Human antibody | EPA antibody | EPO antibody | Erythroid Potentiating Activity antibody | Erythroid-potentiating activity antibody | Fibroblast collagenase inhibitor antibody | FLJ903
规格或纯度 ExactAb™, Validated, 2.6 mg/mL
宿主种属 兔(Rabbit)
特异性 TIMP1
种属反应性 人(Human)
免疫原 A synthetic peptide derived from human TIMP1 (AA 1-207).
阳性对照 WB: HT-29, SK-OV-3 and HeLa cell lysates.
偶联 Unconjugated

产品属性

克隆类型 多克隆抗体
Format Whole IgG
亚型 Rabbit IgG
SDS-PAGE 150 kDa
纯化方法 Protein A purified
物理外观 Liquid
储存缓冲液 10mM PBS, 150mM NaCl, 50% Glycerol, 0.05% BSA, 0.02% Sodium azide, pH 7.4
防腐剂 0.02% Sodium azide
浓度 2.6 mg/mL
储存温度 -20°C储存,避免反复冻融
运输条件 超低温冰袋运输
稳定性与储存 4°C 短期储存(1-2 周)。-20°C下长期保存(24个月)。收货后建议分装。避免冷冻/解冻循环。
分子类型 抗体

关联靶点(人)

TIMP1 Tbio 金属蛋白酶抑制剂1(Metalloproteinase inhibitor 1) (0 活性数据)
活性类型 活性值-log(M) 作用机制 期刊 参考文献(PubMed IDs)

图片

TIMP1 Antibody (Ab131327) - Western Blot
All lanes: TIMP1 Antibody (Ab131327) at 1/1000 dilution
Samples: Lysates at 20 µg per lane
Secondary: Goat Anti-Rabbit IgG H&L (HRP) (Ab170144) at 1/20000 dilution

Predicted band size: 23 kDa
Observed band size: 28 kDa
Exposure time: 1.0 s

应用

应用名称 稀释比例
WB

1/500-1/1000

质检证书(CoA,COO,BSE/TSE 和分析图谱)

C of A & Other Certificates(BSE/TSE, COO):
输入批号以搜索分析图谱:

技术文档和文章

蛋白质印迹的一抗选择指南
Guidelines of Primary Antibodies for Western Blotting
Guidelines of Primary Antibodies for Western Blotting
高分子量蛋白质印迹法
Protocol of Western Blotting For High Molecular Weights
Protocol of Western Blotting For High Molecular Weights
Protocol of Western Blotting For High Molecular Weights
Protocol of Western Blotting For High Molecular Weights

引用文献

1. O'Shea, M M and 7 more authors..  (1992)  Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13..  Biochemistry,  (27): [PMID:1420137]
2. Van Ranst, M M and 7 more authors..  (1991)  The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers..  Cytokine,  [PMID:1653055]
3. Osthues, A A, Knäuper, V V, Oberhoff, R R, Reinke, H H and Tschesche, H H..  (1992)  Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid..  FEBS letters,  (13): [PMID:1730286]
4. Williamson, R A RA and 9 more authors..  (1990)  Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)..  The Biochemical journal,  (1): [PMID:2163605]
5. Rapp, G G and 6 more authors..  (1990)  Characterization of three abundant mRNAs from human ovarian granulosa cells..  DNA and cell biology,  [PMID:2171551]
6. Carmichael, D F DF and 6 more authors..  (1986)  Primary structure and cDNA cloning of human fibroblast collagenase inhibitor..  Proceedings of the National Academy of Sciences of the United States of America,  [PMID:3010309]
7. Docherty, A J AJ and 7 more authors..  (1985)  Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity..  Nature,  [PMID:3903517]
8. Opbroek, A A, Kenney, M C MC and Brown, D D..  (1993)  Characterization of a human corneal metalloproteinase inhibitor (TIMP-1)..  Current eye research,  [PMID:7507419]
9. Knäuper, V V, López-Otin, C C, Smith, B B, Knight, G G and Murphy, G G..  (1996)  Biochemical characterization of human collagenase-3..  The Journal of biological chemistry,  (19): [PMID:8576151]
10. Knäuper, V V and 7 more authors..  (1997)  The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction..  The Journal of biological chemistry,  (21): [PMID:9065415]
11. Hardcastle, A J AJ, Thiselton, D L DL, Nayudu, M M, Hampson, R M RM and Bhattacharya, S S SS..  (1997)  Genomic organization of the human TIMP-1 gene. Investigation of a causative role in the pathogenesis of X-linked retinitis pigmentosa 2..  Investigative ophthalmology & visual science,  [PMID:9286280]
12. Gomis-Rüth, F X FX and 11 more authors..  (1997)  Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1..  Nature,  (4): [PMID:9288970]
13. Wu, B B and 7 more authors..  (2000)  NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases..  Journal of molecular biology,  (14): [PMID:10623524]
14. Zhang, Zemin Z and Henzel, William J WJ..  (2004)  Signal peptide prediction based on analysis of experimentally verified cleavage sites..  Protein science : a publication of the Protein Society,  [PMID:15340161]
15. Lewandrowski, Urs U, Moebius, Jan J, Walter, Ulrich U and Sickmann, Albert A..  (2006)  Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach..  Molecular & cellular proteomics : MCP,  [PMID:16263699]
16. Liu, Tao T and 6 more authors.. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry..  Journal of proteome research,  [PMID:16335952]
17. Ramachandran, Prasanna P and 5 more authors..  (2006)  Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry..  Journal of proteome research,  [PMID:16740002]
18. Jung, Ki-Kyung KK, Liu, Xu-Wen XW, Chirco, Rosemarie R, Fridman, Rafael R and Kim, Hyeong-Reh Choi HR..  (2006)  Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein..  The EMBO journal,  (6): [PMID:16917503]
19. Iyer, Shalini S, Wei, Shuo S, Brew, Keith K and Acharya, K Ravi KR..  (2007)  Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1..  The Journal of biological chemistry,  (5): [PMID:17050530]
20. Grossman, Moran M and 6 more authors..  (2010)  The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function..  Biochemistry,  (27): [PMID:20545310]
21. Batra, Jyotica J and 5 more authors..  (2012)  Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure..  The Journal of biological chemistry,  (4): [PMID:22427646]
22. Rosenow, Anja A and 6 more authors..  (2012)  Resveratrol-induced changes of the human adipocyte secretion profile..  Journal of proteome research,  (7): [PMID:22905912]
23. Toricelli, Mariana M, Melo, Fabiana H M FH, Peres, Giovani B GB, Silva, Débora C P DC and Jasiulionis, Miriam G MG..  (2013)  Timp1 interacts with beta-1 integrin and CD63 along melanoma genesis and confers anoikis resistance by activating PI3-K signaling pathway independently of Akt phosphorylation..  Molecular cancer,  (25): [PMID:23522389]
24. Lee, Soo Youn SY and 9 more authors..  (2014)  TIMP-1 modulates chemotaxis of human neural stem cells through CD63 and integrin signalling..  The Biochemical journal,  (1): [PMID:24635319]
25. Tagliabracci, Vincent S VS and 14 more authors..  (2015)  A Single Kinase Generates the Majority of the Secreted Phosphoproteome..  Cell,  (18): [PMID:26091039]
26. Gasson, J C JC and 9 more authors..  (1985)  Molecular characterization and expression of the gene encoding human erythroid-potentiating activity..  Nature,  [PMID:3839290]

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