VAT1 Human
Vesicle Amine Transport Protein 1 Homolog Human Recombinant
Cat. No.
BT29385
Source
E.coli.
Synonyms
Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.
Appearance
Sterile Filtered colorless solution.
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
VAT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393 a.a.) and having a molecular mass of 44.1kDa.
VAT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
VAT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
VAT1 (Synaptic vesicle membrane protein VAT-1 homolog) is a protein belonging to the quinone oxidoreductase family, specifically the zinc-containing alcohol dehydrogenase subfamily. This protein is found in synaptic vesicles, which are responsible for managing the storage and release of neurotransmitters within nerve terminals. VAT1 expression is known to increase in response to calcium ions, particularly in glioblastomas and during wound healing in basal keratinocytes. As an abundant integral membrane protein in cholinergic synaptic vesicles, VAT1 is thought to play a role in vesicular transport.
Description
Recombinant Human VAT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 413 amino acids. This protein encompasses amino acids 1 to 393 and has a molecular weight of 44.1 kDa. For purification purposes, a 20 amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.
Physical Appearance
A clear, colorless solution that has been sterilized through filtration.
Formulation
The VAT1 protein solution has a concentration of 0.5 mg/ml and is prepared in a buffer containing 20 mM Tris-HCl (pH 8.0), 1 mM DTT, 10% glycerol, and 100 mM NaCl.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For longer storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity is determined to be greater than 90% using SDS-PAGE analysis.
Synonyms
Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDEREVAEA ATGEDASSPP PKTEAASDPQ HPAASEGAAA AAASPPLLRC LVLTGFGGYD KVKLQSRPAA PPAPGPGQLT LRLRACGLNF ADLMARQGLY DRLPPLPVTP GMEGAGVVIA VGEGVSDRKA GDRVMVLNRS GMWQEEVTVP SVQTFLIPEA MTFEEAAALL VNYITAYMVL FDFGNLQPGH SVLVHMAAGG VGMAAVQLCR TVENVTVFGT ASASKHEALK ENGVTHPIDY HTTDYVDEIK KISPKGVDIV MDPLGGSDTA KGYNLLKPMG KVVTYGMANL LTGPKRNLMA LARTWWNQFS VTALQLLQAN RAVCGFHLGY LDGEVELVSG VVARLLALYN QGHIKPHIDS VWPFEKVADA MKQMQEKKNV GKVLLVPGPE KEN.
Product Science Overview
Origin and Discovery
Structure and Function
The amino acid sequence of VAT-1 indicates that it belongs to the NAD(P)-dependent quinone oxidoreductase subfamily. This suggests that VAT-1 may possess enzymatic activity in unknown redox processes . The three-dimensional structure of human VAT-1 has been determined in both the free state and the NADP-bound state, revealing that VAT-1 forms a dimer with a conserved NADPH-binding cleft on each protomer .
Biological Roles
VAT-1 has been implicated in several cellular processes, including:
- Vesicular Transport: VAT-1 is involved in the regulation of vesicular transport, which is crucial for neurotransmitter storage and release .
- Mitochondrial Fusion: VAT-1 has been identified as a mitofusin-binding protein that modulates mitochondrial fusion .
- Phospholipid Transport: VAT-1 plays a role in the phosphatidylserine transport process, enabling mitochondria to receive phosphatidylserine from the endoplasmic reticulum .
- Cell Migration: VAT-1 has been implicated in cell migration and is considered a potential target for anticancer drugs .
Recombinant Human VAT-1
Clinical and Research Implications
VAT-1 has been studied for its potential role in cancer cell motility. A natural polyenone, neocarzilin A, produced by Streptomyces carzinostaticus, functions as a potent inhibitor of cancer cell motility by targeting VAT-1-controlled pathways . Additionally, VAT-1’s involvement in mitochondrial fusion and phospholipid transport makes it a significant protein for understanding cellular metabolism and signaling.
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