Recombinant Mouse Tenascin Protein

Beta LifeScience SKU/CAT #: BLA-10115P

Recombinant Mouse Tenascin Protein

Beta LifeScience SKU/CAT #: BLA-10115P
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Product Overview

Host Species Mouse
Accession Q80YX1
Synonym Cytotactin Glioma associated extracellular matrix antigen GMEM GP 150 225 Hexabrachion HXB JI Myotendinous antigen Neuronectin Tenascin C TenascinC TN TN C TNC
Description Recombinant Mouse Tenascin Protein was expressed in Mammalian. It is a Protein fragment
Source Mammalian
Molecular Weight 241 kDa
Purity >90% by SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth when provided to neurons in culture. May play a role in supporting the growth of epithelial tumors. Ligand for integrins ITGA8:ITGB1, ITGA9:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells.
Subcellular Location Secreted, extracellular space, extracellular matrix.
Protein Families Tenascin family
Database References
Tissue Specificity Expressed in kidney, aortic valve, corneal limbus, periosteum around the ribs, cerebellum, stomach and intestine. High levels of isoform 2 in lung and brain of newborn mice. High levels of isoform 5 in thymus, moderate levels in brain of newborn and adult

Gene Functions References

  1. TNC causes post-subarachnoid hemorrhage neuronal apoptosis and neuroinflammation. PMID: 29546590
  2. Results identify tenascin-C as an endogenous danger signal that is upregulated in systemic sclerosis and drives TLR4-dependent fibroblast activation, and by its persistence impedes fibrosis resolution. PMID: 27256716
  3. ATF3 promotes macrophage migration and reverses M1polarized macrophages to the M2 phenotype by upregulation of TNC via the Wnt/betacatenin signaling pathway. PMID: 28714032
  4. housing of TnC-/- mice in enriched environment abolished hyperlocomotion, led to faster habituation to novel environment, strengthened the grasp of fore limbs and partially improved movement coordination, while the swimming ability remained deficient PMID: 28549651
  5. The synaptic plasticity occurs in the hippocampus of freely behaving mice that lack tenascin-C, the informational content stored by synaptic plasticity is not the same. PMID: 28512860
  6. Study suggests that tenascin-C (TnC) contributes to the regulation of structural plasticity in the cerebellum and that interactions between TnC and matrix metalloproteinase 9 are likely to be important for these processes to occur. PMID: 27089885
  7. the exact role of TNC in primary tumor growth PMID: 28874093
  8. A deficiency of tenascin C interferes with Th1 and Th17 cells, protecting animals from experimental autoimmune encephalomyelitis. PMID: 27974153
  9. secreted by transdifferentiated retinal pigment epithelial cells and promotes the development of choroidal neovascularization via integrin alphaV in a paracrine manner PMID: 27668890
  10. Tenascin-C may be an important mediator in the development of brain edema and blood-brain barrier disruption following subarachnoid hemorrhage, mechanisms for which may involve MAPK-mediated MMP-9 induction and ZO-1 degradation PMID: 26473781
  11. TN-C aggravates autoimmune myocarditis by driving the dendritic cell activation and Th17 differentiation via toll-like receptor 4. PMID: 25376187
  12. TNC supports the stress-induced expression of extracellular matrix that reinforce the aorta and the stress-induced excessive inflammatory response in the aorta. PMID: 24514259
  13. TNC plays an important role in TMJ wound healing, especially for wounds generated by mechanical stress. PMID: 25578971
  14. Tenascin-C is required for normal Wnt/beta-catenin signaling in the whisker follicle stem cell niche. PMID: 25196097
  15. TNC downregulates Dickkopf-1 (DKK1) promoter activity through the blocking of actin stress fiber formation, activates Wnt signaling, and induces Wnt target genes in tumor and endothelial cells. PMID: 24139798
  16. The increased levels of elastin, type V collagen and tenascin C are probably the result of increased expression by fibroblastic cells; reversely, elastin influences myofibroblast differentiation PMID: 24291458
  17. Elevated tenascin-C expression in globoid cell leukodystrophy modified microglial functional response to psychosine. PMID: 25192051
  18. Tenascin-C-derived peptide TNIIIA2 highly enhances cell survival and platelet-derived growth factor (PDGF)-dependent cell proliferation through potentiated and sustained activation of integrin alpha5beta1. PMID: 24808173
  19. FHL2-deficient mice developed a severe and long-lasting lung pathology due to enhanced expression of tenascin C and impaired activation of inflammation-resolving macrophages. PMID: 24260575
  20. the CD34-positive whisker follicle stem cell niche contains both tenascin-C and tenascin-W, and these glycoproteins might play a role in directing the migration and proliferation of these stem cells PMID: 24101721
  21. It is upregulated in inflammation and induces further inflammatory responses and the functional inhibition exerts beneficial effects on AD pathogenesis, suggesting a potential for tnc as a new therapeutic target in AD. PMID: 23673309
  22. Tenascin C did not play an essential role in stem and progenitor cell homing to BM, but significantly altered lymphoid primed progenitor cell homing PMID: 24084079
  23. TNC does not appear to contribute directly to outflow resistance in the eye. PMID: 23882691
  24. TNC expression controls eotaxin level in apo E-/- mice; this chemokine plays a key role in the development of atherosclerosis PMID: 23433402
  25. This study provided evidence that the tenascin-c modulates synaptogenesis and long-term synapse stability. The mutant neurons display reduced frequencies of mEPSCs and mIPSCs. PMID: 23637166
  26. cleavage by gingipains directly affects the biological activity of both fibronectin and tenascin-C in a manner that might lead to increased cell detachment and loss during periodontal disease. PMID: 23313574
  27. Tenascin-C enables macrophage translation of proinflammatory cytokines upon lipopolysaccharide activation of toll-like receptor 4 (TLR4) and suppresses the synthesis of anti-inflammatory cytokines. PMID: 23084751
  28. These data unveil a protective role for tenascin C (TNC) in atherosclerosis and suggest that TNC signaling may have the potential to reduce atherosclerosis, in part by modulating VCAM-1 expression. PMID: 22300502
  29. TNC is involved in the etiopathology of obesity via visceral adipose tissue inflammation representing a link with extracellular matrix remodeling. PMID: 22851489
  30. Both cycling G2-phase cells and early post-mitotic neurons were significantly increased in the retina due to Tnc-deficiency. Further investigations suggested that Tnc regulates these processes via the Wnt-signaling cascade. PMID: 22691363
  31. This study provided evidence that the tenascin-C affect the repair of the blood-spinal cord barrier repair in soinal cord injury. PMID: 22473292
  32. Mice lacking TN-C (TN-C(-/-)) mice showed normal steady-state hematopoiesis; however, they failed to reconstitute hematopoiesis after bone marrow ablation and showed high lethality. PMID: 22553313
  33. data establish a role for BMP, Wnts, and mechanical loading in the regulation of tenascin expression in osteoblasts PMID: 21751239
  34. Tnc deficiency interfered with VCAM-1 vascular deposition and down-regulation of PECAM-1, disrupted MMP-9-positive leukocyte infiltration, hampered apoptosis and necrosis, and favored liver repair/regeneration after ischemia-reperfusion injury. PMID: 21898491
  35. TN-C may be a useful biomarker for indicating the pathological status of smooth muscle cells and interstitial cells in abdominal aortic aneurysm. PMID: 21951663
  36. The data implicated tenascin C in the regulation of proliferation and lineage progression of astroglial progenitors in specific domains of the developing spinal cord. PMID: 22071102
  37. Data show that reduction in metastasis due to the loss of S100A4(+) fibroblasts correlated with a concomitant decrease in the expression of several ECM molecules and growth factors, particularly Tenascin-C and VEGF-A. PMID: 21911392
  38. Promoter-reporter and chromatin immunoprecipitation experiments unraveled a SAP-dependent, SRF-independent interaction of MKL1 with the proximal promoter region of TNC. PMID: 21705668
  39. Tenascin-C is expressed in neural stem cells and neural cells derived from embryonic stem cells where it is expected to have a specific functional role in facilitating nervous tissue repair and regeneration. PMID: 20689858
  40. Study suggests a new role of tenascin-C as a regulator of the fibrinolytic system. PMID: 21354146
  41. Overexpression of TNC-fnD via adeno-associated virus in wild-type mice improved locomotor recovery, increased monaminergic axons sprouting, and reduced lesion scar volume after spinal cord injury. PMID: 20606643
  42. HNK-1 epitope-carrying tenascin-C spliced variant regulates the proliferation of mouse embryonic neural stem cells. PMID: 20855890
  43. Tenascin-C is required for injury-induced epithelial-mesenchymal transition in the mouse lens epithelium. PMID: 20664686
  44. Mechanisms are presented of the first signaling pathways that underlie Tnc-induced, extracellular matrix-dependent maintenance of the immature state of oligodendendrocyte precursor cells. PMID: 20844127
  45. Tenascin-C may thus accelerate adverse ventricular remodeling, cardiac failure, and fibrosis in the residual myocardium after myocardial infarction. PMID: 20081106
  46. Here we show that periostin, a matricellular protein, promotes incorporation of tenascin-C into the extracellular matrix and organizes a meshwork architecture of the extracellular matrix. PMID: 19887451
  47. These findings indicate a role for tenascin-C in structural organization of the CA1 hippocampal subfield and in shaping neural activity. PMID: 19280660
  48. results suggested that the isoforms containing one or five alternatively spliced domains play important roles in the healing process of glomerulonephritis PMID: 12009782
  49. TN-C is involved in hippocampus-dependent contextual memory and synaptic plasticity; the FN6-8 domain is one of molecular determinants mediating these functions. PMID: 12359159
  50. TN-C induces MMP-9 expression directly and by collaboration with TGF-beta in breast cancer progression PMID: 12672030


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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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