LDHB

Lactate Dehydrogenase B Recombinant
Cat. No.
BT11071
Source
Escherichia Coli.
Synonyms
Lactate Dehydrogenase, LDH.
Appearance
Sterile lyophilized powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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

The DNA encoding chicken LDH-B is cloned from cDNA library of chicken heart.

Product Specs

Introduction
Lactate dehydrogenase (LDH) is an enzyme found in many organisms, such as plants and animals. It helps convert pyruvate to lactate and vice versa. This enzyme is important for energy production. In animals, there are different types of LDH.
Description
This product contains the LDH-B gene from chicken heart. The gene was obtained from a cDNA library.
Physical Appearance
Dry powder, free from bacteria.
Formulation
The protein was freeze-dried with a small amount of potassium phosphate. The final concentration is 1 mg/ml.
Solubility
To use, dissolve the LDH powder in sterile 18 megaohm-centimeter H2O to a concentration of at least 100 micrograms/ml. You can then dilute it further with other solutions as needed.
Stability
The LDH powder is stable at room temperature for 3 weeks. For long-term storage, keep it dry and below -18 degrees Celsius. After dissolving the powder, store the solution at 4 degrees Celsius for up to 7 days. For longer storage, keep it below -18 degrees Celsius. Avoid repeated freezing and thawing.
Purity
The purity is over 95%, confirmed by two methods: (a) RP-HPLC and (b) SDS-PAGE.
Biological Activity
The protein's specific activity is 258 units per milligram of protein.
Unit Definition
One unit of activity means 1 micromole of NAD+ is produced per minute at 25 degrees Celsius and pH 7.0. This includes both transaminase activities and a-hydroxyglutarate dehydrogenase activity.
Synonyms
Lactate Dehydrogenase, LDH.
Source
Escherichia Coli.

Product Science Overview

Structure and Function

LDHB is one of the isoforms of lactate dehydrogenase, which exists as a tetramer composed of different combinations of two subunits: LDHA and LDHB. The B isoform is predominantly found in the heart and red blood cells, where it facilitates the conversion of lactate to pyruvate, a key step in the Cori cycle. This cycle is vital for maintaining glucose homeostasis in the body.

Recombinant Production

Recombinant LDHB is produced using genetic engineering techniques. The gene encoding LDHB is cloned into an expression vector, which is then introduced into a host organism, typically E. coli. The host cells are cultured, and the recombinant protein is expressed and subsequently purified. This method allows for the production of large quantities of LDHB with high purity and activity .

Applications

Recombinant LDHB has several applications in research and clinical diagnostics:

  1. Cancer Research: LDHB is a marker for certain types of cancer. Its expression levels can provide insights into the metabolic state of cancer cells, which often exhibit altered glycolysis pathways.
  2. Cardiac Health: Given its abundance in the heart, LDHB levels can be indicative of cardiac health and are used in the diagnosis of myocardial infarction.
  3. Biochemical Studies: LDHB is used in various biochemical assays to study enzyme kinetics and metabolic pathways.
Clinical Significance

The altered metabolism in cancer cells, known as the Warburg effect, often involves a shift to aerobic glycolysis with increased lactate production. LDHB plays a significant role in this process, making it a valuable target for cancer diagnostics and therapeutics .

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