Rabbit Epilysin (MMP-28) Polyclonal Antibody | anti-MMP-28 antibody

Anti-Epilysin (MMP-28), Propeptide Region Antibody

Cat. Num. AAA4157364

• Gene Names: MMP28; MM28; MMP25; MMP-25; MMP-28; EPILYSIN
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot
• Purity: Immunogen Affinity Purified
• Synonyms: Epilysin (MMP-28); Polyclonal Antibody; Anti-Epilysin (MMP-28); Propeptide Region Antibody; anti-MMP-28 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This antibody is specific for MMP28, but does not cross react with the other MMP family members (MMP-1, MMP-2, MMP-3, MMP-9, etc.).
• Purity/Purification: Immunogen Affinity Purified
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)
• Sequence Length: 13

• Applicable Applications for anti-MMP-28 antibody: Western Blot (WB)
• Application Notes: MMP-28 was first cloned from human skin keratinocytes, and named Epilysin to reflect its potential role in remodeling of epidermis. The same group identified MMP-28 in testis, as well as heart, brain, placenta, lung, prostate, intestine and colon. Transcripts of 2.6, 2.0 and 1.2 kb were reported, perhaps representing alternatively spliced forms. MMP-28 was also cloned from human lung, and was detected in lung, kidney, brain, skeletal muscle, and several tumor cell lines. A mouse MMP-28 has been sequenced, and it contains two inserts of 41 and 39 amino acids respectively, relative to the human sequence. The two human sequences (isoform 1, isoform 2) encode proteins of 520 and 393 amino acids, with predicted mass of 58.886 and 44.469 kD respectively. The mouse sequence is predicted to yield a 70.077 kD protein. Promoter analysis suggests that MMP-28 may be constitutively produced in some cells, or that regulation is different from most other MMPs. MMP-28 also has a furin cleavage site, like MMP-11, and is likely cleaved by the prohormone convertase family of enzymes. Sequence homology between MMP-28 and other MMPs is low overall, most closely resembling MMP-19 (at 39% identity). RP1MMP-28 Anti-MMP-28 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 62 Kd and 58 Kd, as well as breakdown products_recover at 50, 48 and 46 kD. The antibody also detects a 70 kD in rat and mouse tissues, which likely represents the larger proform. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Although the sequence homology for this portion of MMP-28 is well conserved, higher concentrations of antibody may be needed for non-human samples.
• Immunogen: Synthetic peptide based on the propeptide region of the Human MMP28 sequence.
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use.; For extended storage, aliquot contents and freeze at-20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Testing Data

Related Product Information for anti-MMP-28 antibody

Description: The antibody is a Rabbit antibody to the Matrix Metalloproteinase Epilysin (MMP-28), made with a synthetic peptide based on the propeptide region of the Human sequence. The antibody binds to MMP-28, but does not cross react with the other MMP family members (MMP-1, MMP-2, MMP-3, MMP-9, etc.). The antibody has been peptide-affinity purified, concentrated to 1 mg/ml, with the addition of sodium azide as preservative and 50% glycerol as cryoprotectant.

Relevance: The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc-endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C-terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. MMPs contain the motif His-Glu-X-X-His (X represents any amino acid) that binds zinc in the catalytic site, as well as another zinc molecule and two calcium molecules structurally. They fall within the matrixin subfamily and are EC designated 3.4.24.x. This group also contains astacin, reprolysin, and serralysin, as well as other more divergent metalloproteinases. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. Matrix Metalloproteinase 28, also known as epilysin, was first cloned from human skin keratinocytes and described to reflect its role in the remodeling of the epidermis. It was found in testis, as well as heart, brain, placenta, lung, prostate, intestine, and colon. MMP28 was later cloned from human lung and found in lung, kidney, brain, skeletal muscle, and several tumor cell lines. At least three MMP28 transcripts of 2.6, 2.0, and 1.2 kb have been reported possibly representing alternatively spliced forms of MMP28. There are two human sequences (isoform1 and isoform 2) which encode proteins of 520 and 393 amino acids with predicted masses of 58.9 and 44.5 kDa respectively. The mouse sequence contains two inserts of 41 and 39 amino acids respectively, relative to the human sequence. Mouse epilysin has a predicted molecular mass of approx. 70 kDa. Mouse and human epilysin are highly conserved and share 97% identical residues. Epilysin (MMP-28) contains the key domains of the other MMPs: a signal peptide, conserved cysteine-containing prodomain (with a furin cleavage site), conserved histidine-containing catalytic domain, hinge domain, and hemopexin domain. MMP28 has a furin cleavage site, similar to MMP11, and is cleaved by the prohormone convertase family of enzymes. Sequence identity between MMP28 and the other MMPs is low overall. MMP28 is most closely related to MMP19 (39% sequence identity). Recombinant MMP28 degrades casein. EDTA and batimastat (selective MMP inhibitor) inhibits the proteolytic activity of epilysin. MMP28 is expressed in tumors as well as normal adult and fetal tissues. It is involved in homeostasis, wound repair, and cell proliferation (during epithelial repair). The MMP28 gene maps to chromosome 17q11.2 and includes 8 exons and 7 introns.

NCBI and Uniprot Product Information

• NCBI GI #: 16224044
• NCBI GeneID: 79148
• NCBI Official Full Name: epilysin, partial
• NCBI Official Synonym Full Names: matrix metallopeptidase 28
• NCBI Official Symbol: MMP28
• NCBI Official Synonym Symbols: MM28; MMP25; MMP-25; MMP-28; EPILYSIN
• NCBI Protein Information: matrix metalloproteinase-28

NCBI Description

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, such as asthma and metastasis. This gene encodes a secreted enzyme that degrades casein. Its expression pattern suggests that it plays a role in tissue homeostasis and in wound repair. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Apr 2014]