Analytical Data
-
Gene name
CLASP2
- Application
-
Alternative Names
CLASP2；KIAA0627；CLIP-associating Protein 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O75122
-
Expression Region
1-431aa
-
AA Sequence
MRRLICKRICDYKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSAGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRSGRLGAGALNAGSYASLECEAFWRSGRTAKLYSV
-
Molecular Weight
60.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 member of the CLASP protein family, which plays a crucial role in microtubule stabilization and cellular processes such as cell division and migration. Research has shown that CLASP2 participates in various cellular functions, including spindle formation, chromosome alignment, and cytoskeletal dynamics, making it vital for proper cellular function and development. Abnormalities in CLASP2 expression have been linked to several diseases, including cancer, as they can lead to defective cell division and tumorigenesis. Investigating the recombinant expression of CLASP2 allows for a better understanding of its structural and functional properties, facilitating the exploration of its role in cellular mechanisms and disease states. The production of recombinant CLASP2 provides an opportunity to study its interaction with other proteins and microtubules in vitro, enabling insights into its regulatory functions and potential as a therapeutic target. Additionally, the recombinant form can be utilized in structural biology studies, such as crystallography or cryo-electron microscopy, to elucidate its three-dimensional structure and molecular interactions. Overall, the research on CLASP2 recombinant protein is significant for advancing our understanding of microtubule dynamics and identifying potential avenues for therapeutic intervention in diseases associated with its dysregulation.
