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- Table of Contents
1 Citations 6 Q&As
Facts about Integrin-linked protein kinase.
Focal adhesion protein part of the complex ILK-PINCH. This complex is thought of as one of the convergence points of integrin- and growth factor-signaling pathway.
Human | |
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Gene Name: | ILK |
Uniprot: | Q13418 |
Entrez: | 3611 |
Belongs to: |
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protein kinase superfamily |
59 kDa serine/threonine-protein kinase; DKFZp686F1765; EC 2.7.11.1; ESTM24; ILK; ILK1; ILK-1; ILK2; ILK-2; integrin-linked kinase; integrin-linked kinase-2; integrin-linked protein kinase; p59; p59ILK
Mass (kDA):
51.419 kDA
Human | |
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Location: | 11p15.4 |
Sequence: | 11; NC_000011.10 (6603708..6610874) |
Highly expressed in heart followed by skeletal muscle, pancreas and kidney. Weakly expressed in placenta, lung and liver.
Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium. Cytoplasm, myofibril, sarcomere.
Boster Bio offers a high affinity ILK antibody with wide range of applications. This antibody is not only highly specific but is also trusted and widely cited by the research community. As a result, it is highly relevant and has been validated for Western Blotting, Immunohistochemistry, and ELISA. Here are some of its most popular uses.
The ILK marker, a cell-surface receptor, is associated with tumor grade. It is expressed within tumor cells and controls p300/p53. It is also a protooncogene and regulates the stability cell cycle inhibitor P27. Boster has validated its antibodies and its reagents on Western Blotting, Immunohistochemistry, and ELISA.
The antisera in Boster Bio that target the cluster differentiation 86 react with Rat and Mouse. They can be kept at 4°C for one month or frozen at 20°C for six months. Boster Bio Anti CD86 Antibody Picoband includes trehalose and rat CD86 Recombinant Protein. This antisera can also be purchased with blocking peptides. These peptides are available in different price ranges depending on the length of your immunogen.
CD antigens are also known as CD marker and play many roles in an organism's immune response. They can be used as receptors, ligands or initiating signal cascades. Some CD-antigens do not affect cell signaling. Instead, they perform other functions. All types and types of cells can recognize a molecule that CD Antigens recognize.
The primary purpose of the CD nomenclature classification is to classify molecules that exhibit the same cellular reactivity. For example, the CD2 mAb reacts with the 50-kDa transmembrane glycoprotein found on resting T cells. Later, the concept was expanded to include many other types of cell. When two specific antibodies bind to the proposed molecules, they are assigned a CD number.
While chemotherapy remains the most effective treatment option for human cancers and is still the most preferred, many chemotherapy therapies are not capable of treating cancers. This means that finding mutations in a tumor's genetic code may improve the treatment. One gene implicated in drug resistance is Skp2, which is expressed in many human cancers. It also mediates resistance against the anti-cancer drug TRAIL.
The F-box family of proteins consists of a 40-amino acid motif named after cyclin F. These proteins form one of four subunits of the Skp1-Cullin-F-box complex, which determines the specificity of the SCF core protein. F-box proteins are adaptor proteins and recruit phosphorylated substrate protein into the SCF core. These proteins contain two domains fundamental to their function: the Fbox motif and the LRR domain.
CDh2 is downregulated, which leads to SKP2 upregulation in HCC, breast cancer and colorectal carcinoma. The ILK detection of SKP2 is a valuable diagnostic tool to help patients with cancer. SKP2 can be used to identify high-risk patients during treatment.
Skp2 expression in ESCC can be used in a variety of ways to identify patients at higher risk for recurrence. The IHC can be used to detect Skp2 expression from tumor tissues. This can help clinicians stratify patients based upon their risk of developing recurrence. This study is not yet complete and further research is needed to determine the effect of ESCC Skp2 on treatment.
Skp2 is a transcriptional gene that ubiquitinates C-Myc, increasing its G1/S transition activity and transactivation activity. This inhibition has been shown to be beneficial in breast cancer. Skp2 overexpression inhibited metastasis of the lung. On the other hand, Skp2 overexpression facilitated breast cancer metastasis.
Skp2 has multiple regulatory mechanisms. A reduction in both SCF2 and Skp2 will be critical for a controlled cell-cycle. Skp2 targets the negative cell cycle regulators to ensure that a controlled cell cycle is achieved. This results in a cell cycle that is orchestrated. The drug will be more active if Skp2 expression is lower in a tumor.
Breast cancer is another application for Skp2 immunohistochemistry. Follicular lymphoma refers to a form of cancer involving B cells that is found in the follicle centre. It is divided into grades according to the number of centroblasts found in the tumor. The abnormalities in cell-cycle regulators may be closely linked to the proliferation of neoplastic cells. Skp2 positively regulates Gl–S transition and promotes degradation cyclin-dependentkinase inhibitor, p27. Recent research suggests that Skp2 may play a role in lymphogenesis as well as carcinogenesis.
The Skp2 genome was amplified, and the vector pcDNA3.1 was cloned with Lipofectamine 2000. The target sequence for the Skp2 gene was 5'-CGCTGCCCACCATTTAT. The miR-339 targeted site was 5’-GGGTCCCTCCTTCGAT. To normalize Skp2's expression, the U6 marker has been used.
PMID: 8538749 by Hannigan G.E., et al. Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase.
PMID: 10871859 by Janji B., et al. Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation.
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