hlp 3

CYP3A4 is an important member of the cytochrome P450 enzyme superfamily, with 33 allelic variants. Human cytochrome P450 3A4 (CYP3A4) is an important drug metabolizing enzyme involved in a number of drug-drug and food-drug interactions. Systemic inflammation has been linked to suppressed CYP3A4 activity.

Hippocalcin-Like Protein 1 (HPCAL1) is a neuron-specific calcium-binding member of the recoverin family which found in the retina and brain. HPCAL1 contains four EF-hand domains and it is highly similar to human hippocalcin protein. HPCAL1 is involved in the calcium-dependent regulation of rhodopsin phosphorylation. In addition, it may be of relevance for neuronal signalling in the central nervous system.

SHH Protein, Human, Recombinant (aa 1-197, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 21 kDa and the accession number is Q15465.

SHH Protein, Human, Recombinant (aa 198-462, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 29 kDa and the accession number is Q15465.

VILIP-1, also known as VSNL1, is strongly expressed in 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. VILIP-1 gene is a member of the visinin/recoverin subfamily of neuronal calcium sensor proteins. Alternatively spliced transcript variants have been observed, but their full-length nature has not been determined.

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.