Analytical Data
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Gene name
COL6A3
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简介
COL6A3 protein is an important component of type VI collagen and has the function of a cell-binding protein. Collagen VI trimers are composed of three distinct chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI), alpha-5(VI), or alpha-6(VI). COL6A3 Protein, Human (HEK293) is the recombinant human-derived COL6A3 protein, expressed by HEK293 , with tag free.
- Application
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Alternative Names
Collagen alpha-3(VI) chain; COL6A3
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Species
Human
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12111-1
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Expression Region
T3101-T3177
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Protein Length
Partial
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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
Moesin is a member of the ERM (ezrin, radixin, moesin) protein family, which plays a crucial role in linking the plasma membrane to the actin cytoskeleton, thereby participating in various cellular processes such as cell shape maintenance, motility, and signaling. It is particularly important in epithelial and endothelial cells, where it contributes to the formation of microvilli and the regulation of cell adhesion. Research into moesin's structure and function has gained momentum due to its implications in numerous physiological and pathological contexts, including cancer progression, metastasis, and immune responses. The study of recombinant moesin protein has allowed researchers to delve deeper into its mechanistic roles, as well as its interactions with other cellular components. By producing and purifying recombinant moesin, scientists can investigate its functional properties in vitro, explore its binding affinities with lipids and proteins, and study its post-translational modifications. Understanding how moesin operates at a molecular level may also provide insights into the development of therapeutic strategies aimed at diseases associated with ERM proteins, making this research area both timely and significant.
