Anti-MMP-9 Antibody, Rabbit Polyclonal sinobiological 80049-T24

$143.00
In stock
SKU
80049-T24
Catalog No.SizePrice (USD)
80049-T24-5050 µL$147.96
80049-T24-100100 µL$251.64
80049-T24-200200 µL$355.32

General Information

Product nameAnti-MMP-9 Antibody, Rabbit Polyclonal
Validated applicationsELISA (FAQ Protocol), IHC-P (FAQ Protocol)
Species reactivityReacts with: Rat
SpecificityRat MMP-9
ImmunogenRecombinant Rat MMP-9 / MMP9 Protein (Catalog#80049-R08H)
PreparationProduced in rabbits immunized with purified, recombinant Rat MMP-9 / MMP9 (rR MMP-9 / MMP9; Catalog#80049-R08H; EDL96479.1; Met1-Pro708). MMP-9 / MMP9 specific IgG was purified by Rat MMP-9 / MMP9 affinity chromatography.
SourcePolyclonal Rabbit IgG
PurificationProtein A & Antigen Affinity
Formulation0.2 μm filtered solution in PBS
ConjugateUnconjugated
FormLiquid
ShippingThis antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
StorageThis antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Synonyms: Anti-Mmp9 Antibody

Image / Experimental Information

Image 1 DescriptionImmunochemical staining of rat MMP9 in rat spleen with rabbit polyclonal antibody (1:1000, formalin-fixed paraffin embedded sections).
Image 1 Alt TextRat MMP9/MMP-9/CLG4B Immunohistochemistry(IHC) 3110
Image 1 URLSource image

Background Information

Full Namematrix metallopeptidase 9
DescriptionMatrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and some transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodeling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent on the delicate balance between MMPs and their inhibitors, excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence, regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. Besides, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
Research Areas
  • Cancer Drug Targets
Related Pathways
  • IL17 signaling pathway
References
  1. St-Pierre Y, et al. (2003) Emerging features in the regulation of MMP-9 gene expression for the development of novel molecular targets and therapeutic strategies. Curr Drug Targets Inflamm Allergy. 2(3): 206-15.
  2. St-Pierre Y, et al. (2004) Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and inflammatory diseases. Expert Opin Ther Targets. 8(5): 473-89.
  3. Chakrabarti S, et al. (2005) Matrix metalloproteinase-2 (MMP-2) and MMP-9 in pulmonary pathology. Exp Lung Res. 31(6): 599-621.

title: Biosensing Intestinal Alkaline Phosphatase by Pregnancy Test Strips Based on Target-Triggered CRISPR-Cas12a Activity to Monitor Intestinal Inflammation.
authors: Zhenzhen Jia; Yujie Zhang; ...; Mingzhen Zhang
journal: Analytical Chemistry
date: 2023-09-20
pmid: 37668549
doi: 10.1021/acs.analchem.3c03099
cited_by_count: 4
techniques: CRISPR; Pregnancy Test (hCG) Assay; Stripping Membranes
bioz_score: 91

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