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Mouse Anti-Porcine IgM μ Chain Specific Monoclonal Antibody-[Biotin]

Cat. No.VD7N432

Product TypeAnimal-targeted Antibodies

Size 1mL

Product Overview

BioVenic mouse monoclonal antibody is specific for porcine IgM μ chain. It can be applied to FCM, IF, IP, IHC, ELISA and WB assays of porcine IgM.

Specifications

Application FCM; IF; IP; IHC; ELISA; WB
Clonality Monoclonal
Classification Labeled Antibody
Clone L14N7
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Porcine IgM
Purity > 90%
Concentration 1 mg/mL
Conjugation Biotin
Preservative and Stabilizer Sodium Azide
Buffer 0.01M Phosphate Buffered Saline, 0.5% Bovine Serum Albumin and 50% Glycerol
Physical State Liquid

Target Information

Porcine IgM μ chain is a crucial component of the immune system in pigs, playing a significant role in the primary immune response. It is characterized by its high molecular weight and a pentameric structure, consisting of five subunits and a single J-chain. Each subunit comprises a pair of heavy (μ) and light chains, with the heavy chain containing one variable and four constant regions. IgM is often referred to as a macroglobulin due to its large size and is the first antibody to be produced in response to an initial exposure to an antigen. It is particularly effective at activating the complement system, a critical part of the immune response that helps to clear pathogens. The μ chain of porcine IgM is also significant in the context of vaccine development and understanding disease resistance in pigs.

Target Porcine IgM μ Chain

Shipping and Storage

This product is shipped with wet ice packs. Store at -20°C on receipt (up to 12 months). Avoid exposure to light. Avoid repeated freezing and thawing as this may denature the antibody.

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. Rungelrath, Viktoria, et al. "IgM cleavage by Streptococcus suis reduces IgM bound to the bacterial surface and is a novel complement evasion mechanism." Virulence 9.1 (2018): 1314-1337.
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