VAPB Human

VAMP Associated Protein B and C Human Recombinant
Cat. No.
BT6137
Source
Escherichia Coli.
Synonyms
Vesicle-associated membrane protein-associated protein B/C, VAMP-B/VAMP-C, VAMP-associated protein B/C, VAP-B/VAP-C, VAPB, ALS8, VAP-B, VAMP-B.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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

VAPB Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 242 amino acids (1-222 a.a.) and having a molecular mass of 27.1kDa (molecular size on SDS-PAGE will appear higher). 
The VAPB is purified by proprietary chromatographic techniques.

Product Specs

Introduction
VAMP-associated protein B (VAPB), also known as vesicle-associated membrane protein (VAMP)-associated protein B, is a type IV transmembrane protein classified under the VAP protein family. It is believed to play a role in vesicle trafficking. Existing as both a homodimer and a heterodimer with VAPA, VAPB is located in the membranes of plasma and intracellular vesicles. It interacts with VAMP1 and VAMP2. Notably, defects in VAPB are linked to the development of amyotrophic lateral sclerosis type 8 and spinal muscular atrophy autosomal dominant Finkel type.
Description
Recombinant human VAPB, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 242 amino acids (1-222 a.a.) with a 20 amino acid His tag fused at the N-terminus, resulting in a molecular mass of 27.1 kDa. Note that the molecular size on SDS-PAGE may appear higher. The purification of VAPB is achieved through proprietary chromatographic techniques.
Physical Appearance
A colorless solution that has been sterilized by filtration.
Formulation
The provided VAPB solution has a concentration of 1 mg/ml and is prepared in a buffer containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the VAPB protein is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms
Vesicle-associated membrane protein-associated protein B/C, VAMP-B/VAMP-C, VAMP-associated protein B/C, VAP-B/VAP-C, VAPB, ALS8, VAP-B, VAMP-B.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGI IDAGASINVS VMLQPFDYDP NEKSKHKFMV QSMFAPTDTS DMEAVWKEAK PEDLMDSKLR CVFELPAEND KPHDVEINKI ISTTASKTET PIVSKSLSSS LDDTEVKKVM EECKRLQGEV QRLREENKQF KEEDGLRMRK TVQSNSPISA LAPTGKEEGL ST.

Product Science Overview

Structure and Function

VAPB is primarily found in the plasma and intracellular vesicle membranes, where it exists as both a homodimer and a heterodimer with VAPA . The protein interacts with VAMP1 and VAMP2, playing a crucial role in vesicle trafficking . VAPB is also involved in the unfolded protein response (UPR), a cellular stress response related to the endoplasmic reticulum (ER) . This response helps in maintaining cellular homeostasis by inducing ERN1/IRE1 activity .

Disease Associations

Mutations in the VAPB gene have been linked to several neurodegenerative diseases. Notably, VAPB is associated with Amyotrophic Lateral Sclerosis 8 (ALS8) and Spinal Muscular Atrophy, Late-Onset, Finkel Type . These conditions are characterized by progressive muscle weakness and atrophy due to the degeneration of motor neurons.

Research and Applications

Human recombinant VAPB is used extensively in research to study its role in cellular processes and disease mechanisms. The protein’s involvement in vesicle trafficking and the UPR makes it a significant target for understanding neurodegenerative diseases and developing potential therapeutic interventions .

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Source
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