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。
MMP13 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- 文献引用 : 2
- 实验流程
- 背景知识
Application 
| WB, IF, IHC-P, E |
|---|---|
| Primary Accession | P45452 |
| Other Accession | O62806, NP_002418.1 |
| Reactivity | Human |
| Predicted | Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 53820 Da |
| Antigen Region | 253-282 aa |
| Gene ID | 4322 |
|---|---|
| Other Names | Collagenase 3, 3424-, Matrix metalloproteinase-13, MMP-13, MMP13 |
| Target/Specificity | This MMP13 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 253-282 amino acids from the Central region of human MMP13. |
| Dilution | WB~~1:1000 IF~~1:10~50 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 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 | MMP13 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MMP13 |
|---|---|
| Function | Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion. |
| Cellular Location | Secreted, extracellular space, extracellular matrix. Secreted |
| Tissue Location | Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue |
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 MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
REFERENCES
Miranda, K.J., et al. J. Biol. Chem. 285(41):31517-31524(2010)
Romero, R., et al. Am. J. Obstet. Gynecol. 203 (4), 361 (2010) :
Nikopensius, T., et al. Birth Defects Res. Part A Clin. Mol. Teratol. 88(9):748-756(2010)
Yamada, T., et al. Anticancer Res. 30(7):2693-2699(2010)
Jugessur, A., et al. PLoS ONE 5 (7), E11493 (2010) :
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