Abcam, ab256485, Anti-Chondroitinase ABC I antibody [HL2010]

Size: 100µg / 1mg
Mouse Recombinant Monoclonal Chondroitinase ABC I antibody. Suitable for I-ELISA, WB and reacts with Proteus vulgaris, Recombinant full length protein - Proteus vulgaris samples. Cited in 2 publications.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:HL2010,
Isotype:IgG1,
Carrier free:No,
Reacts with:Proteus vulgaris,
Applications:I-ELISA, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 30% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, 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.
Chondroitinase ABC I also known as ChABC or Chondroitinase breaks down chondroitin sulfate and dermatan sulfate chains which are components of proteoglycans in the extracellular matrix. This enzyme with an approximate mass of 120 kDa originates from the bacterium Proteus vulgaris. Researchers often focus on its enzymatic function due to its ability to digest glycosaminoglycans thereby reducing inhibitory structures in the nervous system. Chondroitinase ABC I is not endogenously expressed in human tissue but its application involves tissue cultures and animal models.
Biological function summary
This enzyme plays a significant role in modulating the extracellular matrix by cleaving glycosaminoglycans removing barriers that can hinder cell regeneration. This activity indicates its potential for enhancing neural plasticity and aiding tissue repair particularly within the central nervous system. Although not requiring a complex for its activity Chondroitinase ABC I operates effectively in environments where its substrate is present facilitating processes important for remodeling the extracellular matrix.
Pathways
Chondroitinase ABC I contributes to the neural regeneration and repair pathway by altering the extracellular environment. Its function complements the actions of matrix metalloproteinases which also modify the extracellular matrix. The modulation of inhibitory proteoglycans aligns Chondroitinase ABC I with neuroplasticity pathways influencing neurite outgrowth and synaptic remodeling. This activity creates potential for pathways aiming at recovery from neural injuries and degeneration.
The use of Chondroitinase ABC I demonstrates potential therapeutic applications for conditions like spinal cord injury and multiple sclerosis. By facilitating neural repair and overcoming chondroitin sulfate proteoglycan-induced inhibition it offers promise in these challenging conditions. In the context of spinal cord injury Chondroitinase ABC I interacts functionally with proteins related to axonal regeneration such as Nogo receptor supporting its regenerative capability. In multiple sclerosis the enzyme's ability to alter the extracellular matrix may relieve some of the inhibitory effects faced during remyelination efforts.