Rabbit Xenopus Collagenase Polyclonal Antibody

Anti-Xenopus Collagenase (Collagenase-4, MMP-18), Hinge Region MMP-18 Antibody

Cat. Num. AAA4157326

• Applications: Western Blot
• Purity: Immunogen Affinity Purified
• Synonyms: Xenopus Collagenase; Polyclonal Antibody; Anti-Xenopus Collagenase (Collagenase-4; MMP-18); Hinge Region MMP-18 Antibody; MMP-18; anti-Xenopus Collagenase antibody

• Host: Rabbit
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This antibody binds to all forms of MMP18, latent and active, reduced and non-reduced. It does not cross react with the other MMP family members (MMP1, MMP2, MMP3, MMP9).
• Purity/Purification: Immunogen Affinity Purified
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)

• Applicable Applications for anti-Xenopus Collagenase antibody: Western Blot (WB)
• Application Notes: MMP-18 was first described in Xenopus during development, and is distinct from MMP-1, which it most closely resembles. MMP-18 has been shown to digest intact type-I collagen at the same site as the classical collagenases (MMP-1, MMP-8, MMP-13). RP2MMP18 Anti-MMP18 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 53 Kd and 51 Kd (the pro-form), as well as the smaller activated forms. RP2MMP18 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA uses. Collagenase-4 is produced at very low levels in normal, quiescent Xenopus cells and tissues. Collagenase production can be induced by mitogens such as TPA or TNF-a in receptive cell types. Although MMP-18 has been reported in Xenopus tissues, no human orthologue has been identified to date. 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-1 is well conserved, higher concentrations of antibody may be needed for non-human samples.
• Immunogen: Synthetic peptide corresponding to the hinge region of Xenopus laevis MMP18.
• 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-Xenopus Collagenase antibody

Description: The antibody is a Rabbit antibody to the Matrix Metalloproteinase Collagenase-4(Xenopus Collagenase; MMP-18), made with a synthetic peptide based on the hinge region of Xenopus MMP-18. The antibody binds to all forms of MMP-18, latent and active. The antibody binds to Collagenase-4, but does not cross react with the other MMP family members (MMP-1, MMP2, MMP3, MMP9). 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: All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell matrix interactions. MMPs are are a family of at least eighteen secreted and membrane bound zinc endopeptidases that degrade various components of the ECM, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. 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. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis, and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). TIMPs have been shown to block tumor cell invasion suggesting that they act as metastasis suppressor genes. Numerous studies have shown that there is a close association between expression of various members of the MMP family by tumors, and their proliferative and invasive behavior and metastaic potential. MMP18 was first described in Xenopus during development, and is distinct from MMP1, which it most closely resembles. MMP18 is expressed in very low levels in quiescent cells and tissues. MMP18 production can be induced by mitogens such as TPA or TNF alpha in receptive cell types. MMP18 has been shown to digest intact type I collagen at the same site as the classical collagenases (MMP1, MMP8, MMP13).