Exalpha Biologicals, Inc.

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FIX&PERM Cell Fixation and Permeabilization Kit

Flow cytometric analyses with monoclonal antibodies were so far mainly restricted to cell surface molecules. Intracellular structures such as cytoplasmic or nuclear enzymes, oncoproteins, cytokines, immunoglobulins etc. were largely excluded from such studies. Also excluded from flow cytometric studies were cytoplasmic localizations of well-established membrane molecules like CD3 and CD22, which, in their cytoplasmic form, are the most reliable lineage markers in undifferentiated leukemia. With the FIX&PERM® Kit flow cytometric analysis of intracellular antigens has become as easy as surface antigen studies. The only prerequisite is the availability of suitable antibody conjugates. Most of the available monoclonal antibody conjugates can be used with the FIX&PERM® Kit, some determinants are sensitive, however, to the fixation step involved. This and the optimal fixation time have to be tested for each reagent.

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We are pleased to announce that Peter Rutten has now started in his role as Operations Director here at Exalpha Biologicals Inc. Peter has a Master’s of Science degree in Industrial and Organizational Psychology and this has lead him down a very business orientated career path. Peter is looking forward to working with the team at Exalpha. Peters primary focus is the customer experience and he will be working with the Laboratory team, the Quality Control team and the Order Processing team to ensure this focus is achieved. We all wish Peter well in his new role.

Exalpha Biologicals, Inc.

Active Matrix Metalloproteinase 9 (MMP9)

  • Product Code: X2057M
  • Size: 200 µg
  • Availability: In Stock In Stock
  • Price (USD): $232

Cat #

X2057M		 Quantity:      

Data Sheet

Product Name

Active Matrix Metalloproteinase 9 (MMP9)

Synonyms

CLG4B, GELB, 92 kDa gelatinase, matrix metallopeptidase 9

Host/Source

Mouse

Clone

4A3

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 N-terminus of the human MMP9 protein and mouse myeloma Ag8563 cells. Sequence common in rabbit, dog and pig

Positive Control

Esophageal adenocarcinoma. Only present in tumor tissues.

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

63 kDa

Product Image

Image Legend

Left: Immunohistochemical staining of paraffin embedded esophageal tumors using Act-MMP9 antibody (Cat. No. X2057M). Right: Western blot using MMP9 antibody on recombinant human proenzyme MMP9 (left lane) and activated enzyme (right 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