Analytical Data
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Gene name
CHODL
- Application
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Alternative Names
CHODL；C21orf68；Chondrolectin
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Species
Mouse
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9CXM0
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Expression Region
1-216aa
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AA Sequence
MIRIASLLLG AALLCAQGAF ARRVVSGQKV CFADVKHPCY KMAYFHELSS RVSFQEARLA CESEGGVLL SLENEAEQKL IESMLQNLTK PGTGISDGDF WIGLLRSGDG QTSGACPDLY QWSDGSSSQ FRNWYTDEPS CGSEKCVVMY HQPTANPGLG GPYLYQWNDD RCNMKHNYIC KYEPEIHPT EPAEKPYLTN QPEETHENVV VTEAGIIPN
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Molecular Weight
23 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CHODL (Chondroitin sulfate-specific domain containing protein 1) is a relatively underexplored protein that belongs to the family of chondroitin sulfate proteoglycans, which are known for their critical roles in cell signaling, extracellular matrix integrity, and cellular interactions. Research into CHODL has garnered attention due to its potential implications in developmental processes, tissue remodeling, and various pathological conditions, including cancer and neurodegenerative diseases. Distinctively, CHODL contains unique structural features and domains that suggest it may have specialized functions in the regulation of cellular behavior and differentiation. Furthermore, its expression patterns in different tissues and its potential interaction with other biomolecules underscore the necessity for detailed studies on its functional roles. Recombinant CHODL protein studies can provide insights into its biochemical properties, interaction networks, and physiological relevance, paving the way for potential therapeutic applications. As researchers increasingly recognize the significance of proteoglycans in health and disease, understanding CHODL's structure and function will be pivotal for elucidating its contributions to biological processes and its prospective role in targeted therapies.
