GAPDH Human, Active

Glyceraldehyde-3-Phosphate Dehydrogenase Human Recombinant, Active
Cat. No.
BT8517
Source
Escherichia Coli.
Synonyms
G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

GAPDH Human Recombinant produced in E. coli is a single polypeptide chain containing 335 amino acids (1-335) and having a molecular mass of 36kDa. The GAPDH is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme crucial for glycolysis, catalyzing the reversible conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. This enzyme, existing as a tetramer of identical 36-kDa subunits, participates in various cellular processes beyond glycolysis, including membrane fusion, microtubule organization, phosphotransferase activity, nuclear RNA export, and DNA replication and repair.
Description
This product consists of the active human GAPDH enzyme, recombinantly produced in E. coli. It is a single polypeptide chain with 335 amino acids (1-335), resulting in a molecular weight of 36kDa. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The GAPDH protein solution has a concentration of 1 mg/ml and is formulated in a buffer consisting of 20mM Tris-HCl (pH 8), 1mM EDTA, 1mM DTT, and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Minimize repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity, a measure of enzyme activity, is greater than 50 units/mg. One unit is defined as the amount of enzyme required to convert 1.0 µmol of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate per minute at pH 8.5 and 37°C.
Synonyms
G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.
Source
Escherichia Coli.
Amino Acid Sequence
MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE.

Product Science Overview

Structure and Function

GAPDH is a tetrameric protein composed of identical subunits. Each subunit contains an active site that binds to the substrate and coenzyme. The enzyme’s activity is essential for the energy-yielding process of glycolysis, which is fundamental for cellular respiration and energy production .

Recombinant GAPDH

Recombinant GAPDH is produced using genetic engineering techniques, where the human GAPDH gene is inserted into a host organism, typically Escherichia coli (E. coli), to express the protein. This recombinant form is often tagged with histidine to facilitate purification and is lyophilized from a buffered solution with stabilizers .

Applications

Recombinant human GAPDH is widely used in biochemical research. It serves as a positive control in experiments involving protein sulfhydration and is used to study protein-protein interactions, cellular localization, and post-translational modifications. Additionally, GAPDH is involved in various non-metabolic processes, including gene expression regulation and apoptosis .

Clinical Relevance

GAPDH expression levels are often used as a reference in gene expression studies due to its consistent expression in various tissues. However, its dysregulation has been observed in several diseases, including cancer and neurodegenerative disorders .

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