Analytical Data
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Gene name
CR
- Application
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Alternative Names
CALB2; CAL2; CAB29; Calbindin 2,29kDa
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22676
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Expression Region
Phe28~Met248
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Molecular Weight
27kDa
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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
The study of CR (cysteine-rich) recombinant proteins has gained significant attention in recent years due to their diverse roles in various biological processes and their potential applications in biotechnology and medicine. CR proteins are characterized by the presence of conserved cysteine residues, which often form disulfide bonds that contribute to their structural stability and functionality. These proteins are commonly involved in important cellular activities such as cell signaling, immune response, and structural support. Their unique properties make CR proteins ideal candidates for therapeutic agents, particularly in the fields of cancer treatment, drug delivery, and vaccine development. Moreover, advances in protein engineering and recombinant DNA technologies have facilitated the production and modification of CR proteins, allowing researchers to optimize their properties and enhance their efficacy. The ability to express these proteins in heterologous systems, such as bacteria, yeast, or mammalian cells, has further accelerated their study, enabling detailed functional assays and structural analyses. As a result, understanding the mechanisms by which CR proteins interact with other biomolecules and exert their biological functions is crucial for harnessing their potential in scientific research and therapeutic applications. This research area continues to evolve, focusing on the elucidation of the structure-function relationship of CR proteins, their role in disease mechanisms, and their potential as targets for drug discovery and development.
