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AB23479

Anti-Mannan Binding Lectin/MBL antibody [6B11]

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(1 Publication)

Mouse Monoclonal Mannan Binding Lectin/MBL antibody. Suitable for ELISA, WB, IHC-P and reacts with Chicken samples. Cited in 1 publication.

View Alternative Names

Mannose-binding protein, MBP, Mannan-binding protein, MBL

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

6B11

Isotype

IgG1

Light chain type

lambda

Carrier free

No

Reacts with

Chicken

Applications

IHC-P, ELISA, WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

This antibody can be used as coating antibody and as detection antibody in a sandwich ELISA on chicken plasma or serum.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Preservative: 0.097% Sodium azide Constituents: PBS, 2.9% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Mannan Binding Lectin often referred to as MBL is an important player in the innate immune system. It is known alternatively as mannose-binding lectin or mannan-binding protein. The mass of MBL is approximately 32 to 34 kilodaltons and it is primarily produced in the liver. MBL circulates in the bloodstream where it can recognize patterns on the surface of pathogens such as bacteria and viruses through its lectin-binding domain. This recognition leads to the activation of other components that play roles in immune response.
Biological function summary

Mannan Binding Lectin serves a significant role in immune defense by binding to carbohydrate structures on pathogens. It is part of a complex known as the lectin pathway of the complement system one of three pathways that activate the complement system to enhance pathogen removal. MBL can activate through a series of proteases leading to opsonization cell lysis and inflammation which are vital responses to infection.

Pathways

Mannan recognition by MBL initiates the lectin pathway an essential component of the complement system. This pathway converges with the classical and alternative pathways to enhance the immune response. MBL works closely with MBL-associated serine proteases (MASPs) particularly MASP-1 and MASP-2 which cleave complement proteins resulting in pathogen opsonization and membrane attack complex formation. These actions are tightly regulated and ensure effective defense against invaders.

Deficiencies or polymorphisms in MBL can lead to increased susceptibility to infections and developmental complications of the immune system. Individuals with low MBL levels may experience recurrent respiratory infections or other bacterial infections due to inadequate complement activation. Moreover variations in the MBL protein have connections with autoimmune diseases such as systemic lupus erythematosus where MBL levels might influence disease severity. In these conditions altered interactions with other immune proteins like C4 and C3 may contribute to pathological responses.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway.
See full target information MBL

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

American journal of cancer research 15:1759-1776 PubMed40371147

2025

Prognostic value, biological role, and mechanisms of LCN2 in childhood acute lymphoblastic leukemia.

Applications

Unspecified application

Species

Unspecified reactive species

Xue Tang,Yuan-Yuan Li,Lin-Jun Tan,Ju Gao,Zhi-Gui Ma,Xia Guo,Ling Gu,Han-Min Liu
View all publications

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