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Rabbit Anti-MMP9/FITC Conjugated antibody
background:
All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell matrix interactions. MMPs are Zn(2+) binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). TIMPs have been shown to block tumor cell invasion suggesting that they act as metastasis suppressor genes.
Function:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large SLCterminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Subunit:
Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.
Subcellular Location:
Secreted, extracellular space, extracellular matrix (Probable).
Tissue Specificity:
Produced by normal alveolar macrophages and granulocytes.
Post-translational 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.
DISEASE:
Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:603932]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.
Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:613073]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
Similarity:
Belongs to the peptidase M10A family.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin-like domains.
Database links:
Entrez Gene: 4318 Human
Entrez Gene: 403885 Dog
Entrez Gene: 17395 Mouse
Entrez Gene: 81687 Rat
Omim: 120361 Human
SwissProt: O18733 Dog
SwissProt: P14780 Human
SwissProt: P41245 Mouse
SwissProt: P50282 Rat
Unigene: 297413 Human
Unigene: 886 Mouse
Unigene: 10209 Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
合成与降解(Synthesis and Degradation)
MMP9亦称IV型胶原酶或明胶酶B,其主要功能为降解IV型胶原。因而它在肿瘤细胞突破基底膜屏障和浸润转移中起重要作用。
目前主要用于各种恶性肿瘤(如乳腺癌、胃肠道癌、卵巢癌、膀胱癌等)中的基底膜检测与转移浸润的研究。细胞外基质在维持正常组织结构与功能以及细胞生长和分化过程中起重要作用。细胞外基质动态平衡的失调与肿瘤细胞侵袭、转移和复发密切相关,基质金属蛋白酶(MMP9)是细胞外基质的降解酶,可降解Ⅳ、Ⅴ、Ⅸ、Ⅺ型胶原,在肿瘤的浸润、转移过程中起重要作用,近年为肿瘤研究的热点。
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