抗MMP-9抗体(Anti-MMP-9, Pro-, Mouse, Rat-Mono, Biotin antibody)
掲載日情報：2021/01/28 現在Webページ番号：27978
MMP-9に対する抗体(Anti-MMP-9, Pro-, Mouse, Rat-Mono, 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
- Related Research Areas
- Related Product & Information
- Citations
価格
[在庫・価格 ：2025年12月03日 16時55分現在]
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Anti-MMP-9, Pro-, Mouse, Rat-Mono(116125), Biotin |
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[在庫・価格 ：2025年12月03日 16時55分現在]
Anti-MMP-9, Pro-, Mouse, Rat-Mono(116125), Biotin
文献数： 3
- 商品コード：BAM909
- メーカー：RSD
- 包装：250μg
- 価格：¥91,000
- 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：Mouse Pro-MMP-9 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#MAB9092，スタンダードとして#909-MM-010を用いる。 別名：92 kDa gelatinase クローン：116125 Genbank No： 4318 Protein Accession No： P41245.1 |
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| 法規制等 | |||
| 保存条件 | -20℃ | 法規備考 | |
| 抗原種 | Mouse | 免疫動物 | Rat |
| 交差性 | Mouse | 適用 | ELISA |
| 標識 | Biotin | 性状 | Protein A/G Affinity Purified |
| 吸収処理 | クラス | IgG | |
| クロナリティ | Monoclonal | フォーマット | |
| 掲載カタログ |
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| 製品記事 | Myeloid-derived Suppressor Cell Marker |
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| 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 | Mouse |
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| Label | Biotin |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant mouse MMP‑9Ala20-Pro730Accession # P41245.1 |
| Source | Monoclonal Rat IgG2A Clone # 116125 |
| Purification | Protein A or G purified from hybridoma culture supernatant |
| Specificity | Detects mouse Pro-MMP-9 in direct ELISAs. Does not detect the mature form of MMP-9. In sandwich ELISAs, no cross-reactivity was observed with recombinant human (rh) MMP-1, rhMMP-2, rhMMP-3, rhMMP-8, rhMMP-10, rhMMP-12, and rhMMP‑13. |
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Applications and Data
| Recommended Concentration | Sample | |
| Mouse Pro-MMP-9 Sandwich Immunoassay | Reagent | |
| ELISA Capture (Matched Antibody Pair) | 2-8 µg/mL | Mouse Pro-MMP‑9 Antibody (Catalog #MAB9092 ) |
| ELISA Detection (Matched Antibody Pair) | 0.5-2.0 µg/mL | Mouse Pro-MMP‑9 Biotinylated Antibody (Catalog #BAM909 ) |
| ELISA Standard | Recombinant Mouse MMP-9 Protein, CF (Catalog #909-MM ) | |
| Please Note: Optimal dilutions should be determined by each laboratory for each application.General Protocolsare available in the Technical Information section on our website. | Preparation and Storage | |
| Reconstitution | Reconstitute at 0.5 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: MMP-9 | Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain. Compared to the human MMP-9 (R&D Systems, Catalog # 911-MP), the mouse enzyme contains extra sequences in the linker region and in the hemopexin-like domain, respectively. |
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| Long Name: | Matrix Metalloproteinase 9 | |
| Entrez Gene IDs: | 4318 (Human); 17395 (Mouse); 81687 (Rat) | |
| Alternate Names: | 92 kDa gelatinase; 92 kDa type IV collagenase; CLG4B; EC 3.4.24; EC 3.4.24.35; Gelatinase B; GELB; macrophage gelatinase; MANDP2; matrix metallopeptidase 9; matrix metalloproteinase 9; matrix metalloproteinase-9; MMP9; MMP-9; type V collagenase | |
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Related Research Areas
| Airway Inflammation and Remodeling | ||
| Alpha Granule Soluble Molecules | ||
| Cancer Biomarkers | ||
| Cell to Cell Adhesion Disassembly During EMT | ||
| Collagen Modifying Enzymes | ||
| Enzymes Secreted by Endothelial Cells | ||
| Extracellular Matrix Remodeling and Cell Migration During EMT | ||
| Gametes and Fertilization | ||
| Inflammatory Mediators | ||
| Mesenchymal Cells and EMT | ||
| Metalloproteases and Regulators | ||
| MMPs, TIMPs and Related Molecules | ||
| Molecules Secreted by VSMC | ||
| Preeclampsia | ||
| Proteolytic Degradation of Amyloid beta | ||
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Related Product & Information
| Background | MMP-9 |
|---|---|
| background_content | Background: MMP-9 Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain. Compared to the human MMP-9 (R&D Systems, Catalog # 911-MP), the mouse enzyme contains extra sequences in the linker region and in the hemopexin-like domain, respectively. |
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Citations
- Brucella abortus induces TNF-alpha-dependent astroglial MMP-9 secretion through mitogen-activated protein kinases.
Authors: Miraglia M, Scian R, Samartino C, Barrionuevo P, Rodriguez A, Ibanez A, Coria L, Velasquez L, Baldi P, Cassataro J, Delpino M, Giambartolomei G
J Neuroinflammation, 2013;10(0):47.
Species: Mouse
Sample Type: Cell Culture Supernates
Application: ELISA detection - Compartment-specific remodeling of splenic micro-architecture during experimental visceral leishmaniasis.
Authors: Yurdakul P, Dalton J, Beattie L, Brown N, Erguven S, Maroof A, Kaye PM
Am. J. Pathol., 2011;179(1):23-9.
Species: Mouse
Sample Type: Whole Cells
Application: Flow
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