Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
MMP17 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q9ULZ9 |
| Other Accession | NP_057239.4 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 66653 Da |
| Antigen Region | 432-460 aa |
| Gene ID | 4326 |
|---|---|
| Other Names | Matrix metalloproteinase-17, MMP-17, 3424-, Membrane-type matrix metalloproteinase 4, MT-MMP 4, MTMMP4, Membrane-type-4 matrix metalloproteinase, MT4-MMP, MT4MMP, MMP17, MT4MMP |
| Target/Specificity | This MMP17 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 432-460 amino acids from the C-terminal region of human MMP17. |
| Dilution | WB~~1:1000 IHC-P~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | MMP17 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MMP17 |
|---|---|
| Synonyms | MT4MMP |
| Function | Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. |
| Cellular Location | [Isoform Long]: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side. Secreted, extracellular space, extracellular matrix |
| Tissue Location | Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non- transformed cell types |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
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 protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage.
References
Romero, R., et al. Am. J. Obstet. Gynecol. 203 (4), 361 (2010) :
Nalpas, B., et al. Gut 59(8):1120-1126(2010)
Romero, R., et al. Am. J. Obstet. Gynecol. 202 (5), 431 (2010) :
Huang, C.H., et al. Neoplasia 11(12):1371-1382(2009)
Atkinson, S.J., et al. Biochem. J. 398(1):15-22(2006)
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
