Analytical Data
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Gene name
CHAD
- Application
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Alternative Names
Cartilage leucine rich Protein; Cartilage leucine-rich Protein; Chad; CHAD_HUMAN; Chondroadherin; Chondroadherin proteoglycan; SLRR4A
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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
Q13111
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Expression Region
1-395aa
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AA Sequence
MVRPMLLLSLGLLAGLLPALAACPQNCHCHSDLQHVICDKVGLQKIPKVSEKTKLLNLQRNNFPVLAANSFRAMPNLVSLHLQHCQIREVAAGAFRGLKQLIYLYLSHNDIRVLRAGAFDDLTELTYLYLDHNKVTELPRGLLSPLVNLFILQLNNNKIRELRAGAFQGAKDLRWLYLSENALSSLQPGALDDVENLAKFHVDRNQLSSYPSAALSKLRVVEELKLSHNPLKSIPDNAFQSFGRYLETLWLDNTNLEKFSDGAFLGVTTLKHVHLENNRLNQLPSNFPFDSLETLALTNNPWKCTCQLRGLRRWLEAKASRPDATCASPAKFKGQHIRDTDAFRSCKFPTKRSKKAGRH
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Molecular Weight
65.89 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
Research on CHAD (Cationic Histone-Associated Domain) recombinant proteins has gained significant attention due to their potential roles in various biological processes. CHAD proteins, characterized by their interaction with histones and involvement in chromatin remodeling, play critical roles in regulating gene expression and cellular functions. These proteins are implicated in several physiological and pathological conditions, including cancer, where epigenetic modifications can lead to tumor progression. The ability to produce recombinant CHAD proteins allows for detailed structural and functional analyses, enabling researchers to explore their mechanisms of action and interactions within the cellular environment. By employing advanced techniques such as site-directed mutagenesis and protein crystallography, scientists aim to elucidate the structural basis of CHAD function, which may reveal new therapeutic targets for interventions in diseases linked to dysregulated gene expression. Additionally, the study of CHAD recombinant proteins can also provide insights into the evolutionary conservation of protein interactions and their significance across different organisms. The continued investigation into CHAD proteins not only enhances our understanding of fundamental biological processes but also paves the way for innovative strategies in biotechnology and medicine.
