| 货号 | 3852 |
| 宿主 | Rabbit |
| 抗原 | synthetic peptide corresponding to residues surrounding Lys115 of human MMP-9 |
| 供应商 | CST |
| 应用范围 | W, IHC-P |
| 适应物种 | H,R |
| 保存条件 | -20°c |
| 是否单克隆 | 单克隆 |
| 级别 | 详见MSDS文件 |
| 抗体英文名 | MMP-9 Antibody |
| 保质期 | 详见说明书 |
| 数量 | 大量 |
| 规格 | 100 ul (10 western blots)/carrier free & custom formulation / quantity |
pathwaymore infoapplication referencesdatasheet PDFMSDS PDFprotocols
Applications Key: W=Western Blotting IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key: H=Human R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IHC-P | H (R) | Endogenous | 84, 92 | Rabbit |
| Protocols | |
|---|---|
| Specificity / Sensitivity | MMP-9 Antibody detects full length (proenzyme, 92 kDa) and cleaved (active enzyme, 84 kDa) MMP-9. |
| Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys115 of human MMP-9. Antibodies are purified by protein A and peptide affinity chromatography. Western BlottingWestern blot analysis of partially purified, concentrated, serum-free medium containing human MMP-9, using MMP-9 Antibody. IHC-P (paraffin)Immunohistochemical analysis of paraffin-embedded human benign meningioma, using MMP-9 Antibody. IHC-P (paraffin)Immunohistochemical analysis of paraffin-embedded human squamous cell carcinoma of the esophagus, using MMP-9 Antibody. |
| Background | The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7 and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis (2-4). MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5). |
| Application References | Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know! |
| Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |