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anti-MMP9 antibody :: Mouse anti-Human MMP-9 Monoclonal Antibody

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Catalog # MBS670154
Unit / Price
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  0.1 mg  /  $265 +1 FREE 8GB USB
Testing Data
Product Name

MMP-9 (MMP9), Monoclonal Antibody

Full Product Name

Mouse Anti-Human MMP-9-UNLB

Product Synonym Names
Mouse Anti-Human MMP-9 - Purified, Unlabeled Antibody; Mouse Anti-Human MMP-9
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 20; NC_000020.10 (44637547..44645200). Location: 20q11.2-q13.1
3D Structure
ModBase 3D Structure for P14780
Mouse IgG2a
Clone Number
Species Reactivity
Human MMP-9; Does not cross react to human MMP-1, MMP-2 or MMP-3
Matrix metalloproteinases (MMPs) are a family of at least 20 structurally related, zinc-containing enzymes that have the ability to breakdown connective tissue. MMP-9 is also known as gelatinase B and 92kDa gelatinase. MMP-9, along with MMP-2, belongs to the gelatinase group of MMP's which have three repeats of a type II fibronectin domain inserted in the catalytic domain. MMP-9 has shown direct and indirect substrate specificity to collagens IV, V, X and XIV, gelatin, elastin, proteoglycans, plasminogen, aggrecan, galectin-3, entactin, fibrillin, fibrin, IL-1 beta, amyloid beta peptide and myelin basic protein. 1-15
Purified (UNLB) Antibody
Recombinant MMP-9
To insure lot-to-lot consistency, each batch of product is tested by ELISA to conform with the characteristics of a standard reference reagent.
Preparation and Storage
The purified antibody (UNLB) is supplied as 0.1 mg purified immunoglobulin in 0.2 mL of 100 mM borate buffered saline, pH 8.2. No preservatives or amine-containing buffer salts added. Store at 2- 8 degree C.
The horseradish peroxidase (HRP) conjugate is supplied as 1.0 mL of stock solution in 50% glycerol/50% PBS, pH 7.4. No preservative added. Store at 2-8 degree C or long-term at -20 degree C.
Reagents are stable for the period shown on the label if stored as directed.
Other Notes
Small volumes of anti-MMP9 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Applications Tested/Suitable for anti-MMP9 antibody
ELISA; Immunohistochemistry_PES
Application Notes for anti-MMP9 antibody
Immunohistochemistry Suggested Dilution: <= 2 ug/mL
ELISA Suggested Dilution: 1:3,000-1:8,000

Testing Data of anti-MMP9 antibody
anti-MMP9 antibody Testing Data image
NCBI/Uniprot data below describe general gene information for MMP9. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
78,458 Da[Similar Products]
NCBI Official Full Name
matrix metalloproteinase-9 preproprotein
NCBI Official Synonym Full Names
matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
NCBI Official Symbol
NCBI Official Synonym Symbols
  [Similar Products]
NCBI Protein Information
matrix metalloproteinase-9; 92 kDa gelatinase; OTTHUMP00000031674; type V collagenase; macrophage gelatinase; 92 kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
UniProt Protein Name
Matrix metalloproteinase-9
UniProt Synonym Protein Names
92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B
Protein Family
UniProt Gene Name
UniProt Synonym Gene Names
CLG4B  [Similar Products]
UniProt Entry Name
NCBI Summary for MMP9
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. [provided by RefSeq]
UniProt Comments for MMP9
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 C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. Ref.16

Catalytic activity: Cleavage of gelatin types I and V and collagen types IV and V. Ref.16

Cofactor: Binds 2 zinc ions per subunit.Binds 3 calcium ions per subunit.

Enzyme regulation: Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Ref.19 Ref.21

Subunit structure: 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. Ref.18 Ref.21 Ref.27

Subcellular location: Secreted › extracellular space › extracellular matrix


Tissue specificity: Produced by normal alveolar macrophages and granulocytes.

Induction: Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Ref.11 Ref.12 Ref.19 Ref.21 Ref.24

Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification: 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. Ref.9

Involvement in 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. Ref.22Defects 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.

Miscellaneous: In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.

Sequence similarities: Belongs to the peptidase M10A family.Contains 3 fibronectin type-II domains.Contains 4 hemopexin-like domains.
Product References and Citations for anti-MMP9 antibody
1. Steffensen, B., U.M. Wallon, and C.M. Overall. 1995. J. Biol. Chem. 270:11555.
2. Allan, J.A., A.J. Docherty, P.J. Barker, N.S. Huskisson, J.J. Reynolds, and G. Murphy. 1995. Biochem. J. 309:229.
3. Murphy, G., M.I. Cockett, R.V. Ward, and A.J. Docherty. 1991. J. Biol. Chem. 277:277.
4. Murphy, G., J.J. Reynolds, U. Bretz, and M. Baggiolini. 1982. Biochem. J. 203:209.
5. Welgus, H.G., C.J. Fliszar, J.L. Seltzer, T.M. Schmid, and J.J. Jeffery. 1990. J. Biol. Chem. 265:13521.
6. Sires, U.I., B. Dublet, E. Aubert-Foucher, M. van der Rest, and H.G. Welgus. 1995. J. Bio. Chem. 270:1062.
7. Patterson, B.C., and Q.A. Sang. 1997. J. Biol. Chem. 272:28823.
8. Fosang, A.J., P.J. Neame, K. Last, T.E. Hardingham, G. Murphy, and J.A. Hamilton. 1992. J. Biol. Chem. 267:19470.
9. Ochieng, J., R. Fridman, P. Nangia-Makker, D.E. Kleiner, L.A. Liotta, W.G. Stetler-Stevenson, and A. Raz. 1994. Biochemistry 33:14109.
10. Sires, U.I., G.L. Griffin, T.J. Brekelmann, R.P. Mecham, G. Murphy, A.E. Chung, H.G. Welgus, and R.M. Senior. 1993. J. Biol. Chem. 268:2069.
11. Ashworth, J.L., G. Murphy, M.J. Rock, M.J. Sherratt, S.D. Shapiro, C.A. Shuttleworth, and C.M. Kielty. 1999. Biochem. J. 340:171.
12. Lelongt, B., S. Bengatta, M. Delauche, L.R. Lund, Z. Werb, and P.M. Ronco. 2001. J. Exp Med. 193:793.
13. Ito, A., A. Mukaiyama, Y. Itoh, H. Nagase, I.B. Thogersen, J.J. Enghild, Y. Sasaguri, and Y. Mori. 1996. J. Biol. Chem. 271:14657.
14. Chandler, S., R. Coates, A. Gearing, J. Lury, G. Wells, and E. Bone. 1995. Neurosci. Lett. 201:223.

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