ELISA/assay

Rabbit tenascin-R ELISA Kit

MBS721863

48-Strip-Wells

470 USD

ELISA Kit

Rabbit tenascin-R ELISA Kit

tenascin-R

Rabbit tenascin-R ELISA Kit; tenascin-R; tenascin-R (Rabbit)

tenascin-R; Tenascin-R; tenascin-R; janusin; restrictin; tenascin R (restrictin, janusin); tenascin R; Janusin; Restrictin

TN-R

TNR; TNR; TN-R; TN-R

TENR_HUMAN

Rabbit

Store all reagents at 2-8 degree C

Rabbit ELISA Kit

157384973

NP_003276.3

NM_003285.2

Q92752

149,562 Da

ECM Proteoglycans Pathway (833812); ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Extracellular Matrix Organization Pathway (576262); Focal Adhesion Pathway (198795); Focal Adhesion Pathway (83067); Focal Adhesion Pathway (478); PI3K-Akt Signaling Pathway (692234); PI3K-Akt Signaling Pathway (692979)

Tenascin-R (TNR) is an extracellular matix protein expressed primarily in the central nervous system. It is a member of the tenascin (TN) gene family, which includes at least 3 genes in mammals: TNC (or hexabrachion; MIM 187380), TNX (TNXB; MIM 600985), and TNR (Erickson, 1993 [PubMed 7694605]). The genes are expressed in distinct tissues at different times during embryonic development and are present in adult tissues.[supplied by OMIM, Mar 2008]

Function: Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance . By similarity. Subunit structure: Forms oligomers. Interacts with CNTN1, TNC, and FN1. Interacts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 . By similarity. Subcellular location: Secreted extracellular space extracellular matrix. Tissue specificity: Brain specific. Ref.1. Domain: The EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B . By similarity. Post-translational modification: Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated carbohydrate structure . By similarity. O-glycosylated on Thr-36 or Thr-37 with a core 1 or possibly core 8 glycan. Sequence similarities: Belongs to the tenascin family.Contains 5 EGF-like domains.Contains 1 fibrinogen C-terminal domain.Contains 9 fibronectin type-III domains.

48-Strip-Wells

470 USD

96-Strip-Wells

675