Recombinant Human Integrin-Linked Protein Kinase (ILK) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10301P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Integrin-Linked Protein Kinase (ILK) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10301P
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Product Overview

Description Recombinant Human Integrin-Linked Protein Kinase (ILK) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q13418
Target Symbol ILK
Synonyms 59 kDa serine/threonine protein kinase; 59 kDa serine/threonine-protein kinase; DKFZp686F1765 ; Epididymis secretory protein Li 28; HEL S 28; ILK 1; ILK 2; ILK; ILK-1; ILK-2; ILK_HUMAN; ILK1; ILK2; Integrin linked kinase 2; Integrin linked Kinase; Integrin linked protein kinase; Integrin-linked protein kinase; p59; p59ILK
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWS
Expression Range 1-228aa
Protein Length Partial
Mol. Weight 30.0kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Regulates cell motility by forming a complex with PARVB. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
Subcellular Location Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium. Cytoplasm, myofibril, sarcomere.
Protein Families Protein kinase superfamily, TKL Ser/Thr protein kinase family
Database References
Tissue Specificity Highly expressed in heart followed by skeletal muscle, pancreas and kidney. Weakly expressed in placenta, lung and liver.

Gene Functions References

  1. Using molecular modeling and molecular dynamics simulations, we show that Asp344, Asp352, and Thr356 in kindlin-2 and Arg243 and Arg334 in ILK kinase domain (KD) are important in kindlin-2/ILK complex formation. Mutations that disrupt these interactions abrogate kindlin-2 and ILK colocalization in HeLa cells. PMID: 29237230
  2. High ILK expression is associated with Neuroblastoma. PMID: 29695398
  3. We further performed molecular dynamics simulation for 100ns to see the effect of urea on structural stability of kinase domain of ILK at atomic level. Structural changes with increasing concentrations of urea were analysed, and we observed a significant increase in the root mean square deviation, root mean square fluctuations, solvent accessible surface area and radius of gyration PMID: 29309873
  4. ILK overexpression in human CRC associates with EMT and CSC traits, contributing to tumor progression and chemoresistance. PMID: 29496692
  5. Dermal fibroblast-to-myofibroblast transition sustained by alphavss3 integrin-ILK-Snail1/Slug signaling is a common feature for hypermobile Ehlers-Danlos syndrome and hypermobility spectrum disorders. PMID: 29309923
  6. These results indicated that ILK promoted cell proliferation and growth in breast cancer cells through activation of the PI3K/Akt pathway. PMID: 28791358
  7. ILK-induced epithelial-mesenchymal transition is a novel mechanism in the pathogenesis of adenomyosis PMID: 29409901
  8. Herein, we propose a new ILK-MMP9-MRTF axis that appears to be critical for endothelial-mesenchymal transition differentiation of endothelial to cancer-associated fibroblasts -like cells. Thus, it might be an attractive target for cancer treatment PMID: 28893556
  9. The current data support MT1-MMP as an additional ILK substrate and show that modulation of ILK expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells. PMID: 26959113
  10. Results show that ILK is overexpressed in metastasis of bladder cancer and the up-regulation of ILK could increase cell proliferation, change cell morphology and regulate cell cycle promoting epithelial-mesenchymal transition. PMID: 27576342
  11. This study is the first to identify EMILIN-1 and ILK as prospective markers of islet regenerative function in human mesenchymal stem cells. PMID: 27090767
  12. ILK aids trophoblast syncytialization via downregulation of CDH1, perhaps through an ILK-PARP1-SNAI1 pathway PMID: 28339614
  13. We conclude that ILK is critical for maintaining the collecting duct epithelium and renal function and is a key intermediate for periostin activation of signaling pathways involved in cyst growth and fibrosis in PKD. PMID: 28522687
  14. Emodin inhibits the migration and invasion abilities of human endometrial stromal cells by by facilitating the mesenchymal-epithelial transition through targeting integrin-linked kinase. PMID: 27130230
  15. Data indicate a regulatory role for tetraspanin 8 (Tspan8) in melanoma progression by modulating cell-matrix interactions through beta1 integrin - integrin-linked kinase (ILK) axis and establish Tspan8 as a negative regulator of ILK activity. PMID: 28188308
  16. Our results define ILK as a key mechanotransducer in modulating breast cancer stem-like cells development in response to tissue mechanics and oxygen tension. PMID: 27503933
  17. Overexpression of ILK therefore promoted the proliferation of SHG44 human glioma cells, reduced apoptosis and reduced sensitivity to TMZ via decreasing the activity of caspase3. PMID: 28138714
  18. iNOS-derived NO plays a crucial role during atherosclerosis by regulating the endocytic-lysosomal degradation of ILK in endothelial cells. PMID: 28546219
  19. Using in vitro studies, we demonstrated that ILK and PI3K/AKT inhibitors suppressed the contraction of fibroblast-populated collagen lattices, inhibited fibroblast migration, and interrupted the effect of TGF-beta1 on promoting alpha smooth muscle actin (alpha-SMA) expression in fibroblasts. PMID: 27111285
  20. During human endometrial decidualization, ILK is essential for morphologic transformation of endometrial stromal cells through organization of the actin cytoskeleton. PMID: 28069177
  21. These data suggest a novel link between Tiam1 and RhoG/ILK /ELMO2 pathway as upstream effectors of the Rac1-mediated phagocytic process in trabecular meshwork cells. PMID: 27539661
  22. silencing of ILK attenuates the abnormal proliferation and migration of human Tenon's capsule fibroblasts induced by TGF-beta2. PMID: 27315599
  23. findings describe a TNFalpha-NF-kappaB-mediated mechanism by which ILK expression is induced in the lymph node microenvironment and propose that ILK promotes leukemogenesis by enabling CLL cells to cope with centrosomal defects acquired during malignant transformation PMID: 26837762
  24. High expression of ILK is associated with bladder cancer. PMID: 27683053
  25. ILK overexpression improved the proliferation, metastasis, and invasion ability of colorectal tumor cells, and this effect may be mediated by the NF-kappaB/rel/A signaling pathway. PMID: 27099440
  26. These findings suggest that emodin inhibited the EMT of EOC cells via ILK/GSK-3beta/Slug signaling pathway PMID: 28097141
  27. periostin enhanced invasion and migration abilities of EECs and facilitated the epithelial-mesenchymal transition of endometrial epithelial cell through ILK-Akt signaling pathway PMID: 27034956
  28. High ILK expression is associated with pancreatic ductal adenocarcinomas. PMID: 26887611
  29. Twist-ITGB1-FAK/ILK pathway and their downstream signaling network dictate the Twist-induced EMT process in human mammary epithelial cells and breast cancer cells PMID: 26693891
  30. Results indicated that ILK is imperative in the development and progression of oral squamous cell carcinoma. PMID: 26531674
  31. Periostin enhanced ensometrial stromal cell migration, invasion, and adhesion due to the ILK1/Akt signal pathway. PMID: 25759370
  32. high extracellular concentration of phosphate induced senescence in cultured smooth muscle through the activation of IGF-1 receptor and ILK overexpression PMID: 26467393
  33. our data suggest an essential role of PINCH1, ILK and ILKAP for the radioresistance of p53-wildtype glioblastoma multiforme cells PMID: 26460618
  34. ILK inhibition and knockdown effects senescence in an Rb-dependent manner. PMID: 26176204
  35. ILK may have an important role in the progression of NSCLC, possibly through up-regulation of Snail and MRP1. PMID: 25964055
  36. integrin linked kinase may play a role in cell proliferation, and cell migration in aggressive thyroid cancers. PMID: 26549818
  37. knockdown of ILK inhibits glioma cell migration, invasion and proliferation through upregulation of E-cadherin and downregulation of cyclin D1. Our results suggest that ILK may serve as a promising therapeutic target for glioma. PMID: 25998224
  38. Overexpression of CD29 decreased E-cadherin, but increased fibronectin, vimentin, ILK activity. PMID: 25805567
  39. Overexpression of ILK is associated with arteriosclerosis. PMID: 26210487
  40. our study shows that ILK regulates the EMT in RCC cells, and targeting ILK suppresses invasion and metastasis through inhibition of the EMT in RCC. PMID: 25657336
  41. PARVA promotes metastasis by modulating ILK signalling pathway in lung adenocarcinoma PMID: 25738875
  42. RNA silencing of ILK increases the sensitivity of the A549 lung cancer cell line to cisplatin and promotes its apoptosis. PMID: 25760437
  43. An increase in integrin-linked kinase non-canonically confers NF-kappaB-mediated growth advantages to gastric cancer cells by activating ERK1/2 PMID: 25398317
  44. ILK activity changes may act as a mechanism in response to different stimuli such as H2O2 in the induced TGF-beta1 up-regulation in pathological or even physiological conditions. PMID: 23624332
  45. ILK mediates cardiomyocyte force transduction through regulation of SERCA-2a and phosphorylation of phospholamban. PMID: 25208486
  46. critical function for ILK in mitotic cytoskeletal organization PMID: 24911651
  47. Thymosin beta4 induces invasion and migration of human colorectal cancer cells through the ILK/AKT/beta-catenin signaling pathway. PMID: 25218472
  48. A major ILK binding site in the kindlin-2 FERM domain for regulating cell adhesion has been mapped. PMID: 25160619
  49. Data demonstrate that p34SEI-1 induces the activation of either AKT or ILK signaling on HER2/neu expression status. PMID: 24789658
  50. A pivotal role of ILK in epithelial-mesenchymal transition and metastasis. PMID: 24360977

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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