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Mouse Anti-Porcine Lactate Dehydrogenase B (LDHB) Monoclonal Antibody

Cat. No.VD8N264

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for lactate dehydrogenase B. It is affinity purified by protein A. It can be applied to WB, IHC, IF and ELISA assays of lactate dehydrogenase B.

Specifications

Application WB; IF; IHC; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G6N8
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Lactate Dehydrogenase B
Isotype IgG1
Immunogen Recombinant protein of lactate dehydrogenase B
Purification Protein A Purified
Concentration 1400 μg/mL
Conjugation Unconjugated
Preservative and Stabilizer 0.02% Sodium Azide
Buffer Phosphate Buffered Saline with 50% Glycerol, pH 7.3
Physical State Liquid

Target Information

Porcine lactate dehydrogenase B (LDHB) is an enzyme that plays a critical role in anaerobic metabolism, specifically in the conversion of pyruvate to lactate during glycolysis. This conversion is essential for maintaining the redox balance and energy production in cells, particularly under conditions where oxygen supply is limited. LDHB is one of the five isoforms of lactate dehydrogenase, each composed of different subunits (A or B). The B subunit, as found in LDHB, is more efficient at converting pyruvate to lactate, which is why LDHB is often more abundant in tissues with high glycolytic activity, such as heart and skeletal muscle.

Target Lactate Dehydrogenase B
Gene ID 102161427
UniProt ID P00336

Shipping and Storage

This product is shipped with ice gel packs. Store at -20°C (up to 12 months) on receipt.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

  1. Liang, Xijun, et al. "Exercise inducible lactate dehydrogenase B regulates mitochondrial function in skeletal muscle." Journal of Biological Chemistry 291.49 (2016): 25306-25318.
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