Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Liposome (VS-1024-FY113)

CAT#: VS-1024-FY113

Anti-MGMT antibody-conjugated liposomes have emerged as a promising therapeutic strategy for targeting gliomas, a notoriously difficult type of brain tumor. These innovative liposomal formulations can enhance drug delivery directly to tumor cells while minimizing collateral damage to healthy tissues, thereby improving treatment efficacy. Recent studies have highlighted the potential of these liposome-based nanomaterials, suggesting they could pave the way for novel approaches in glioma research and development, ultimately leading to more effective clinical treatments.

Gene Expression
Figure 1 IF staining of human cell line U-2 OS Figure 2 IHC staining of human bone marrow Figure 3 IF staining of human cell line A-431 Figure 4 IF staining of human cell line U-251 MG Figure 5 Testis Figure 6 Lymph node Figure 7 RNA cell line category: Cell line enriched (NB-4)
Sub Cat Product Name Liposome Name Datasheet  
VS-1124-FY1905 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Gd-SLs Liposome (VS-1124-FY1905) Gd-SLs liposome
VS-1124-FY1906 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled PEGylated Liposome (VS-1124-FY1906) PEGylated liposome
VS-1124-FY1907 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Triptolide-loaded Liposome (VS-1124-FY1907) Triptolide-loaded liposome
VS-1124-FY1908 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Phospholipid Liposome (VS-1124-FY1908) Phospholipid liposome
VS-1124-FY1909 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Cationic Liposome (VS-1124-FY1909) Cationic liposome
VS-1124-FY1910 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Adriamycin-encapsulated Liposome (VS-1124-FY1910) Adriamycin-encapsulated liposome
VS-1124-FY1911 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Magnetofluorescent Liposome (VS-1124-FY1911) Magnetofluorescent liposome
VS-1124-FY1912 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled pH-sensitive Liposome (VS-1124-FY1912) pH-sensitive liposome
VS-1124-FY1913 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Phototoxic Liposome (VS-1124-FY1913) Phototoxic liposome
VS-1124-FY1914 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Targeted Liposome (VS-1124-FY1914) Targeted Liposome
VS-1124-FY1915 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Apt1-Liposome (VS-1124-FY1915) Apt1-liposome
VS-1124-FY1916 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Thermosensitive Liposome (VS-1124-FY1916) Thermosensitive liposome
VS-1124-FY1917 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Clodronate Liposome (VS-1124-FY1917) Clodronate liposome
VS-1124-FY1918 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Galcer Liposome (VS-1124-FY1918) Galcer liposome
VS-1124-FY1919 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled HBsAg-loaded Liposome (VS-1124-FY1919) HBsAg-loaded liposome
VS-1124-FY1920 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled Phospholipid Liposome and Cationic Liposome (VS-1124-FY1920) Phospholipid liposome and Cationic liposome
VS-1124-FY1921 Anti-MMP9 (clone GS-5745) Recombinant Antibody Coupled ISMN Liposome (VS-1124-FY1921) ISMN liposome
More Infomation

Specifications

  • Potential Clinical Applications
  • Glioma

Product Composition

  • Clone
  • GS-5745
  • Antibody Type
  • IgG
  • Antibody Host
  • Human
  • Antibody Reactivity
  • Human
  • Antibody Description
  • This is a recombinant human monoclonal antibody specifically designed to bind to human matrix metalloproteinase 9 (MMP9). MMP9 is an important enzyme involved in the degradation of extracellular matrix components, playing a significant role in various physiological processes, including tissue remodeling, wound healing, and inflammation.

Product Property

  • Storage
  • See in the COA
  • Storage Shelf Time
  • See in the COA

Target Information

  • Target
  • MMP9
  • Introduction
  • 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. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
  • Alternative Names
  • Matrix Metallopeptidase 9; Matrix Metalloproteinase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); EC 3.4.24.35; CLG4B; MMP-9; GELB; Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); Matrix Metalloproteinase-9
  • Full Name
  • Matrix Metallopeptidase 9
  • Cellular Localization
  • Secreted
  • Post Translation Modifications
  • Processing of the precursor yields different active forms of 64, 67 and 82 kDa.
    Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
    N- and O-glycosylated. (P14780-MMP9_HUMAN)
    Glycosylation at Asn38, Asn120, and Asn127 (NX_P14780 [NX_P14780-1])
    Modification sites at PhosphoSitePlus (P14780)
    Glycosylation from GlyConnect MMP9_HUMAN (6)
    Glycosylation from GlyGen (P14780) 4 sites, 1 N-linked glycan (1 site), 29 O-linked glycans (1 site)
  • Function
  • Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:2551898, 1480034, 12879005).
    Could play a role in bone osteoclastic resorption (By similarity).
    Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005).
    Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094).
    Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034).
    Degrades fibronectin but not laminin or Pz-peptide.
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