癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
MMP24 Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q9Y5R2 |
| Other Accession | Q99PW6, Q9R0S2, NP_006681 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 73231 Da |
| Antigen Region | 396-425 aa |
| Gene ID | 10893 |
|---|---|
| Other Names | Matrix metalloproteinase-24, MMP-24, 3424-, Membrane-type matrix metalloproteinase 5, MT-MMP 5, MTMMP5, Membrane-type-5 matrix metalloproteinase, MT5-MMP, MT5MMP, Processed matrix metalloproteinase-24, MMP24, MT5MMP |
| Target/Specificity | This MMP24 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 396-425 amino acids from the Central region of human MMP24. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| 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 | MMP24 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MMP24 |
|---|---|
| Synonyms | MT5MMP |
| Function | Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity). |
| Cellular Location | [Matrix metalloproteinase-24]: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3 |
| Tissue Location | Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas. |
For Research Use Only. Not For Use In Diagnostic Procedures.
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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, MMP24 is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 by cleavage. The gene has previously been referred to as MMP25 but has been renamed matrix metalloproteinase 24 (MMP24).
REFERENCES
Jung, M., et al., Prostate 55(2):89-98 (2003).
Kajita, M., et al., FEBS Lett. 457(3):353-356 (1999).
Llano, E., et al., Cancer Res. 59(11):2570-2576 (1999).
Nagase, H., et al., J. Biol. Chem. 274(31):21491-21494 (1999).
Kinoh, H., et al., Cytogenet. Cell Genet. 87 (1-2), 97-98 (1999).
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