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C265
Recombinant Human Visinin-like protein 1/HLP3/VSNL1
10ug
1200
1080
现货
国产
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C265
Recombinant Human Visinin-like protein 1/HLP3/VSNL1
50ug
3520
3168
现货
国产
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C265
Recombinant Human Visinin-like protein 1/HLP3/VSNL1
500ug
12320
11088
现货
国产
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C265
Recombinant Human Visinin-like protein 1/HLP3/VSNL1
1mg
17600
15840
现货
国产
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Catalog# C265 Source E.coli Description Recombinant Human Visinin-Like Protein 1/VILIP is produced by our E. coli expression system. The target protein is expressed with sequence (Gly2-Lys191) of Human VSNL1 fused with a His tag at the N-terminus. Names Visinin-Like Protein 1, VILIP, VLP-1, Hippocalcin-Like Protein 3, HLP3, VSNL1, VISL1 Accession # P62760 Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris, 20mM NaCl, pH 8.0 Shipping The product is shipped at ambient temperature. Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in 1X PBS.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.Purity Greater than 95% as determined by reducing SDS-PAGE. Endotoxin Less than 0.1 ng/μg (1 IEU/μg). Amino Acid Sequence MGSSHHHHHHSSGLVPRGSHMGKQNSKLAPEVMEDLVKSTEFNEHELKQWYKGFLKDCPSGRLNL EEFQQLYVKFFPYGDASKFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDL DGDGKITRVEMLEIIEAIYKMVGTVIMMKMNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAA KSDPSIVLLLQCDIQKBackground Visinin-Like Protein 1 (VILIP) is a a member of the Visinin/Recoverin subfamily of neuronal calcium sensor proteins. VILIP is strongly expressed in the Granule Cells of the Cerebellum where it associates with membranes in a Calcium-dependent manner and modulates intracellular signaling pathways of the central nervous system by directly or indirectly regulating the activity of Adenylyl Cyclase. It has been shown that VILIP regulates the inhibition of rhodopsin phosphorylation in a Calcium-dependent manner in vitro.