Analytical Data
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Gene name
ChGn
- Application
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Alternative Names
4-N-acetylgalactosaminyltransferase 1; Beta4GalNAcT 1; beta4GalNAcT; Beta4GalNAcT-1; Beta4GalNAcT1; CGAT1_HUMAN; ChGn; Chondroitin beta-1; Chondroitin beta1 4 N acetylgalactosaminyltransferase; Chondroitin beta1 4 N acetylgalactosaminyltransferase 1; Chondroitin sulfate N acetylgalactosaminyltransferase 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TDX6
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Expression Region
1-297aa
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AA Sequence
MMMVRRGLLAWISRVVVLLVLLCCAISVLYMLACTPKGDEEQLALPRANSPTGKEGYQAVLQEWEEQHRNYVSSLKRQIAQLKEELQERSEQLRNGQYQASDAAGLGLDRSPPEKTQADLLAFLHSQVDKAEVNAGVKLATEYAAVPFDSFTLQKVYQLETGLTRHPEEKPVRKDKRDELVEAIESALETLNNPAENSPNHRPYTASDFIEGIYRTERDKGTLYELTFKGDHKHEFKRLILFRPFGPIMKVENEKLNMANTLINVIVPLAKRVDKFRQFMQNFRPADEVFRCVPLSP
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Molecular Weight
58.41 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
Related Products
Protein Description
ChGn, or Chitinase-like protein, has gained significant attention in recent years due to its potential roles in various biological processes, including inflammation, tissue remodeling, and immune response. Initially identified as a member of the family of chitinases, ChGn is characterized by its unique structure that lacks chitinase activity but retains the ability to bind chitin and other carbohydrate ligands. Research has shown that ChGn is expressed in multiple tissues, and its levels can vary in response to environmental factors and diseases, particularly in conditions such as asthma, rheumatoid arthritis, and certain cancers. The protein's regulatory functions suggest it could be a novel biomarker for disease progression and a potential therapeutic target. Understanding the molecular mechanisms underlying ChGn's function through recombinant protein studies is crucial for uncovering its role in health and disease. Moreover, recombinant ChGn can serve as a valuable tool in biochemical assays and therapeutic applications, enhancing our ability to decipher its intricate involvement in various physiological and pathological processes. The continued exploration of ChGn's properties and functions could not only advance basic biological knowledge but also pave the way for innovative clinical strategies in disease management.











