Recombinant Human TECTB protein (His tag)
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Recombinant Human TECTB protein (His tag) is a Human Fragment protein, in the 1 to 304 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
Beta-tectorin, TECTB
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human TECTB protein (His tag) (AB276695)
SDS-PAGE analysis of ab276695
Reactivity data
Sequence info
Properties and storage information
Form
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The tectorial membrane's function depends on the structural integrity provided by TECTB. It is part of a complex that includes alpha tectorin (TECTA) and other non-collagenous components. Together these proteins form an intricate matrix that maintains the membrane's mechanical properties essential for proper auditory transduction. The complex's ability to transmit sound energy effectively depends on the arrangement of its protein components which TECTB helps stabilize.
Pathways
TECTB plays a role in the mechanotransduction pathway within the auditory system. This pathway involves the conversion of mechanical stimuli into neural signals a process closely associated with proteins such as prestin and myosin VIIA. TECTB's interaction with these proteins ensures the efficient transmission of sound-induced oscillations to the sensory hair cells contributing to hearing function.
General info
Function
One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals.
Post-translational modifications
The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment.
Target data
Product promise
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