规格 | 价格 | 库存 |
---|---|---|
50ul | ¥ 1200 | 7 |
100ul | ¥ 1900 | 6 |
200ul | ¥ 2900 | 3 |
产品编号 | Ys-1377R |
英文名称 | MMP-26 |
中文名称 | 基质金属蛋白酶-26抗体 |
别 名 | MMP26_HUMAN; Endometase; Matrilysin 2; MMP26; Matrix Metalloproteinase 26; MMP 26. |
抗体来源 | Rabbit |
克隆类型 | Polyclonal |
交叉反应 | Human, |
产品应用 | WB=1:500-2000 ELISA=1:5000-10000 IHC-P=1:100-500 IHC-F=1:100-500 IF=1:100-500 (石蜡切片需做抗原修复) not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. |
理论分子量 | 18kDa |
细胞定位 | 分泌型蛋白 |
性 状 | Liquid |
浓 度 | 1mg/ml |
免 疫 原 | KLH conjugated synthetic peptide derived from human MMP26: 185-261/261 |
亚 型 | IgG |
纯化方法 | affinity purified by Protein A |
缓 冲 液 | 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. |
保存条件 | Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. |
注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
PubMed | PubMed |
产品介绍 | Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9. The proteolytic activity was blocked by TIMP1 and TIMP2. MMP26 does not appear to be produced by most normal quiescent cells, but treatment of many cell types with the phorbol ester TPA, or IL1 stimulates production of MMP26. Function: May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B. Subcellular Location: Secreted, extracellular space, extracellular matrix. Tissue Specificity: Expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines. Similarity: Belongs to the peptidase M10A family. |