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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[在庫・価格 :2024年05月18日 00時00分現在]

※ 表示されている納期は弊社に在庫が無く、取り寄せた場合の納期目安となります。
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納期 文献数
Anti-MMP-9, Pro-, Mouse, Rat-Mono(116125), Biotin
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。 3
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
法規制等
保存条件 -20℃ 法規備考
抗原種 Mouse 免疫動物 Rat クラス IgG 標識 Biotin
交差性 Mouse 適用 ELISA
クロナリティ Monoclonal フォーマット 性状 Protein A/G Affinity Purified 吸収処理
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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

[在庫・価格 :2024年05月18日 00時00分現在]

※ 表示されている納期は弊社に在庫が無く、取り寄せた場合の納期目安となります。

Anti-MMP-9, Pro-, Mouse, Rat-Mono(116125), Biotin

文献数: 3

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
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

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 ReactivityMouse
LabelBiotin
ImmunogenMouse myeloma cell line NS0-derived recombinant mouse MMP‑9Ala20-Pro730Accession # P41245.1
SourceMonoclonal Rat IgG2A Clone # 116125
PurificationProtein A or G purified from hybridoma culture supernatant
SpecificityDetects 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 ImmunoassayReagent
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
ReconstitutionReconstitute at 0.5 mg/mL in sterile PBS.Reconstitution Buffer Available
ShippingThe product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & StorageUse 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.

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
  1. 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


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Related Product & Information

BackgroundMMP-9
background_contentBackground:
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

R&D Systems personnel manually curate a database that contains references using R&D Systems products.The data collected includes not only links to publications in PubMed,but also provides information about sample types, species, and experimental conditions.
  1. 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

  2. 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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