VSNL1 Human, His
Visinin-Like Protein-1 Human Recombinant, His Tag
Cat. No.
BT25977
Source
Escherichia Coli.
Synonyms
VISL1, VISL-1, VIS1, VIS-1, VILIP, HLP3, Hippocalcin-like protein 3, VSNL1, VILIP-1, VILIP1, HLP-3, HPCAL3, HUVISL1, Visinin-like protein 1.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
Visinin-Like Protein-1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 23.4 kDa.
Visinin-Like Protein-1 is fused to His tag at N-Terminus.
The protein‘s amino acid sequence corrssponds toUniProtKB/Swiss-Prot entry P62760.
Visinin-Like Protein-1 is purified by proprietary chromatographic techniques.
Visinin-Like Protein-1 is fused to His tag at N-Terminus.
The protein‘s amino acid sequence corrssponds toUniProtKB/Swiss-Prot entry P62760.
Visinin-Like Protein-1 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
VSNL1, a member of the visinin/recoverin family of neuronal calcium sensor proteins, is predominantly expressed in cerebellar granule cells. It exhibits calcium-dependent membrane association and plays a crucial role in regulating central nervous system signaling pathways. VSNL1 modulates adenylyl cyclase activity, impacting cellular processes. Notably, altered VSNL1 expression is observed in the hippocampus of individuals with schizophrenia, indicating its potential involvement in the disorder. Furthermore, VSNL1 is found in pancreatic beta-cells, where it influences insulin secretion through cAMP-dependent mechanisms. Its downregulation has been linked to decreased cAMP accumulation but increased insulin gene transcription. VSNL1 interacts with the cell membrane and actin cytoskeleton, influencing cellular functions. Additionally, VSNL1 modulates cAMP accumulation in C6 glioma cells, while its counterpart, HLP3, affects cGMP accumulation in neural cells and cerebellar granule neurons.
Description
Recombinant Visinin-Like Protein-1, produced in E. coli, is a single, non-glycosylated polypeptide chain with 201 amino acids and a molecular weight of 23.4 kDa. This protein features an N-terminal His tag and corresponds to the UniProtKB/Swiss-Prot entry P62760. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein solution, sterile-filtered and concentrated to 0.5 mg/ml, was lyophilized with 20mM Tris and 20mM NaCl at pH 7.5.
Solubility
To obtain a working concentration of 0.5 mg/ml, reconstitute the lyophilized pellet by adding sterile deionized water and allow for complete dissolution.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. Reconstituted protein can be stored at 4°C for a limited period.
Purity
Greater than 90% purity as determined by SDS-PAGE.
Synonyms
VISL1, VISL-1, VIS1, VIS-1, VILIP, HLP3, Hippocalcin-like protein 3, VSNL1, VILIP-1, VILIP1, HLP-3, HPCAL3, HUVISL1, Visinin-like protein 1.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHAS MGKQNSKLAP EVMEDLVKST EFNEHELKQW YKGFLKDCPS GRLNLEEFQQ LYVKFFPYGD ASKFAQHAFR TFDKNGDGTI DFREFICALS ITSRGSFEQK LNWAFNMYDL DGDGKITRVE MLEIIEAIYK MVGTVIMMKM NEDGLTPEQR VDKIFSKMDK NKDDQITLDE FKEAAKSDPS IVLLLQCDIQK.
Product Science Overview
Structure and Expression
VILIP-1 is expressed in neuronal pericaria, dendrites, and some axons . It is a full-length human protein expressed in Escherichia coli with a His tag at the C-terminus, which facilitates its purification and detection . The recombinant form of VILIP-1 is typically used in various biochemical assays, including SDS-PAGE and sELISA .
Function
Applications
Clinical Relevance
VILIP-1 has emerged as a potential biomarker for various neurological conditions. Its levels in blood and cerebrospinal fluid (CSF) are being studied for their correlation with neurodegenerative diseases . This makes VILIP-1 a valuable target for research in understanding and diagnosing these conditions.
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