Recombinant Mouse Tenascin (TNC) Protein (His&Myc)

Name: Recombinant Mouse Tenascin (TNC) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-03752P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Tenascin (TNC) Protein (His&Myc) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q80YX1
Target Symbol	TNC
Synonyms	Tnc; Hxb; Tenascin; TN; Hexabrachion; Tenascin-C; TN-C
Species	Mus musculus (Mouse)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	GLLYPFPRDCSQAMLNGDTTSGLYTIYINGDKTQALEVYCDMTSDGGGWIVFLRRKNGREDFYRNWKAYAAGFGDRREEFWLGLDNLSKITAQGQYELRVDLQDHGESAYAVYDRFSVGDAKSRYKLKVEGYSGTAGDSMNYHNGRSFSTYDKDTDSAITNCALSYKGAFWYKNCHRVNLMGRYGDNNHSQGVNWFHWKGHEYSIQFAEMKLRPSN
Expression Range	1884-2099aa
Protein Length	Partial
Mol. Weight	28.8 kDa
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	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	KEGG: mmu:21923 UniGene: PMID: 29546590 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 ATF3 promotes macrophage migration and reverses M1polarized macrophages to the M2 phenotype by upregulation of TNC via the Wnt/betacatenin signaling pathway. PMID: 28714032 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 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 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 the exact role of TNC in primary tumor growth PMID: 28874093 A deficiency of tenascin C interferes with Th1 and Th17 cells, protecting animals from experimental autoimmune encephalomyelitis. PMID: 27974153 secreted by transdifferentiated retinal pigment epithelial cells and promotes the development of choroidal neovascularization via integrin alphaV in a paracrine manner PMID: 27668890 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 TN-C aggravates autoimmune myocarditis by driving the dendritic cell activation and Th17 differentiation via toll-like receptor 4. PMID: 25376187 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 TNC plays an important role in TMJ wound healing, especially for wounds generated by mechanical stress. PMID: 25578971 Tenascin-C is required for normal Wnt/beta-catenin signaling in the whisker follicle stem cell niche. PMID: 25196097 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 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 Elevated tenascin-C expression in globoid cell leukodystrophy modified microglial functional response to psychosine. PMID: 25192051 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 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 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 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 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 TNC does not appear to contribute directly to outflow resistance in the eye. PMID: 23882691 TNC expression controls eotaxin level in apo E-/- mice; this chemokine plays a key role in the development of atherosclerosis PMID: 23433402 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 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 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 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 TNC is involved in the etiopathology of obesity via visceral adipose tissue inflammation representing a link with extracellular matrix remodeling. PMID: 22851489 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 This study provided evidence that the tenascin-C affect the repair of the blood-spinal cord barrier repair in soinal cord injury. PMID: 22473292 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 data establish a role for BMP, Wnts, and mechanical loading in the regulation of tenascin expression in osteoblasts PMID: 21751239 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 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 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 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 Promoter-reporter and chromatin immunoprecipitation experiments unraveled a SAP-dependent, SRF-independent interaction of MKL1 with the proximal promoter region of TNC. PMID: 21705668 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 Study suggests a new role of tenascin-C as a regulator of the fibrinolytic system. PMID: 21354146 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 HNK-1 epitope-carrying tenascin-C spliced variant regulates the proliferation of mouse embryonic neural stem cells. PMID: 20855890 Tenascin-C is required for injury-induced epithelial-mesenchymal transition in the mouse lens epithelium. PMID: 20664686 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 Tenascin-C may thus accelerate adverse ventricular remodeling, cardiac failure, and fibrosis in the residual myocardium after myocardial infarction. PMID: 20081106 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 These findings indicate a role for tenascin-C in structural organization of the CA1 hippocampal subfield and in shaping neural activity. PMID: 19280660 results suggested that the isoforms containing one or five alternatively spliced domains play important roles in the healing process of glomerulonephritis PMID: 12009782 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 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.

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