Analytical Data
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Gene name
CLASP2
- Application
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Alternative Names
Cytoplasmic linker-associated protein 2 Protein Orbit homolog 2 Short name: hOrbit2
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Species
Human
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Source
E. coli
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Tag
N- His-B2M
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75122
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Expression Region
1-431aa
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Molecular Weight
60.5 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
CLASP2 (Cytoplasmic Linker Associated Protein 2) is a widely studied protein known for its crucial role in microtubule dynamics and cellular organization. As a member of the CLASP family, CLASP2 is involved in regulating microtubule stability, organization, and interactions with various cellular structures. Its importance is underscored in processes such as cell division, cellular signaling, and the maintenance of cellular architecture. Dysregulation of CLASP2 has been implicated in a variety of diseases, including cancer, where altered microtubule dynamics can promote tumorigenesis and metastasis. Recent research into recombinant CLASP2 protein has focused on elucidating its structure-function relationships, which could provide insights into its regulatory mechanisms and interactions with other cellular components. The ability to produce recombinant CLASP2 allows for detailed biochemical and biophysical studies, opening avenues for potential therapeutic targets and strategies. Understanding the functional roles of CLASP2 at the molecular level can advance our knowledge of microtubule-associated processes and their implications in health and disease. This research is particularly relevant in the development of novel cancer treatment approaches, where targeting microtubule dynamics could offer new therapeutic avenues.
