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MMP9 Polyclonal Antibody

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MMP9 Polyclonal Antibody

Product Details

BS-4593R

Applications
Tested Dilution
Publications

Western Blot (WB)

1:200
-

Immunohistochemistry (Paraffin) (IHC (P))

1:200
-

Immunohistochemistry (Frozen) (IHC (F))

1:100-1:500
-

Immunocytochemistry (ICC/IF)

1:50-1:200
-

Flow Cytometry (Flow)

1:20-1:100
-

ELISA (ELISA)

1:500-1:1,000
-
Product Specifications

Species Reactivity

Dog, Human, Mouse, Rabbit, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

KLH conjugated synthetic peptide derived from human MMP9, amino acids 151-250.
3D Epitope / Immunogen

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Amount

100 µg

Purification

Protein A

Storage buffer

0.01M TBS, pH 7.4, with 50% glycerol, 1% BSA

Contains

0.02% ProClin 300

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

Target Information

MMP9 (matrix metallopeptidase 9, GELB, CLG4B) is a matrix metalloproteinase, a family of zinc and calcium-dependent endopeptidases that degrade extracellular matrix proteins. MMP9 is secreted as a 92kDa zymogen and cleavage of pro-MMP9 results in the active enzyme with a molecular weight of 82kDa. MMP9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 is supplied by bone marrow-derived cells and contributes to skin carcinogenesis. Further, MMP9 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. Studies have shown that elevated MMP9 is associated with progression of idiopathic atrial fibrillation and aortic aneurysm.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: 92 kDa gelatinase; 92 kDa type IV collagenase; 92-kDa type IV collagenase; 92kD gelatinase; 92kD type IV collagenase; CLG4B; collagenase type IVB; gelatinase B; Gelatinase-B; GELB; macrophage gelatinase; matrix metallo protease; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase; matrix metalloproteinase 9; matrix metalloproteinase 9 (gelatinase B, 92-kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase-9; Matrix metalloproteinase9; MMP; MMP-9; MMP-9 proprotein; MMP-9; matrix metalloproteinase 9; MMP9; MMPs; Preproform of 92-kDa type IV collagenase (MMP-9): N-terminal; type IV collagenase MMP-9; type IV MMP-9; type V collagenase; unnamed protein product

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Gene Aliases: B/MMP9; CLG4B; Gel B; GELB; MANDP2; MMP-9; pro-MMP-9

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UniProt ID: (Rabbit) P41246, (Human) P14780, (Rat) P50282, (Mouse) P41245

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Entrez Gene ID: (Rabbit) 100008993, (Dog) 403885, (Human) 4318, (Rat) 81687, (Mouse) 17395

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Function(s)
metalloendopeptidase activity peptidase activity zinc ion binding endopeptidase activity serine-type endopeptidase activity protein binding collagen binding metallopeptidase activity identical protein binding fibronectin binding macromolecular complex binding metalloprotease
Process(es)
proteolysis collagen catabolic process positive regulation of protein phosphorylation cell migration extracellular matrix disassembly extracellular matrix organization macrophage differentiation endodermal cell differentiation negative regulation of apoptotic process positive regulation of DNA binding positive regulation of epidermal growth factor receptor signaling pathway ephrin receptor signaling pathway regulation of multicellular organismal process positive regulation of keratinocyte migration cellular response to lipopolysaccharide cellular response to UV-A positive regulation of release of cytochrome c from mitochondria regulation of neuroinflammatory response negative regulation of cation transmembrane transport response to amyloid-beta positive regulation of vascular smooth muscle cell proliferation negative regulation of epithelial cell differentiation involved in kidney development negative regulation of intrinsic apoptotic signaling pathway skeletal system development ossification response to hypoxia kidney development positive regulation of leukocyte migration response to oxidative stress heart development embryo implantation parturition response to nutrient response to xenobiotic stimulus response to mechanical stimulus response to high light intensity protein catabolic process positive regulation of cell migration positive regulation of synaptic plasticity response to estradiol response to lipopolysaccharide response to retinoic acid response to vitamin A response to tumor necrosis factor response to nicotine positive regulation of apoptotic process response to ethanol positive regulation of angiogenesis negative regulation of fibroblast proliferation macrophage chemotaxis tissue remodeling response to hyperoxia cellular response to iron(III) ion cellular response to cytokine stimulus cellular response to interleukin-1 cellular response to tumor necrosis factor cellular response to low-density lipoprotein particle stimulus cellular response to cell-matrix adhesion modification of synaptic structure, modulating synaptic transmission regulation of postsynaptic neurotransmitter receptor diffusion trapping
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