Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • ELISA
  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.

News

Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

Exalpha Biologicals, Inc.

Matrix Metalloproteinase 9 (MMP9)

  • Product Code: X2056M
  • Size: 200 µg
  • Availability: In Stock In Stock
  • Price (USD): $232

Cat #

X2056M		 Quantity:      

Data Sheet

Product Name

Matrix Metalloproteinase 9 (MMP9)

Synonyms

CLG4B; GELB; 92 kDa gelatinase; matrix metallopeptidase 9

Host/Source

Mouse

Clone

2C3

Isotype

IgG1

Product Type

Monoclonal Antibody

Reactivity

Human

Applications

Western Blot, Immunohistochemistry (Paraffin sections)

Purification

Protein A/G Chromatography

Size

200 µg

Price (USD)

$232

Background

The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92-kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Immunogen

Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminus of the human MMP9 protein and mouse myeloma Ag8563 cells.

Positive Control

Colon, oesophageal and gastric tissues. Stronger expression in tumor versus normal tissue.

Formulation

Provided as solution in phosphate buffered saline with 0.08% sodium azide

Customer Storage

Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight

92 kDa

Product Image

Image Legend

Left: Immunohistochemical staining of paraffin embedded colon carcinoma using MMP9 antibody (Cat. No. X2056M). Antigen retreival using 10mM citrate buffer and microwave method was used. Right: Western blot using MMP9 antibody on recombinant human proenzyme MMP9 (400 ng/lane).

Database Links:

SwissProtP14780Human

References

1. Wang, L. et al. (2006). Matrix metalloproteinase 2 (MMP2) and MMP9 secreted by erythropoietin-activated endothelial cells promote neural progenitor cell migration. J. Neurosci. 26(22);5996-6003

2. Solmiari, S.B., et al. (2006). Circulating MMP2 and MMP9 in breast cancer -- potential role in classification of patients into low risk, high risk, benign disease and breast cancer categories. Int. J. Cancer. 119(6);1403-1411

3. Chen, X., et al. (2005). Increased plasma MMP9 in integrin alpha1-null mice enhances lung metastasis of colon carcinoma cells. Int. J. Cancer. 116(1);52-61