Analytical Data
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Gene name
MAD2L1BP
- Application
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Alternative Names
MAD2L1BP;CMT2;KIAA0110;MAD2L1-binding Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15013
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Expression Region
1-274aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAPEA EVLSSAAVPD LEWYEKSEET HASQIELLET SSTQEPLNAS EAFCPRDCMV PVVFPGPVSQ EGCCQFTCEL LKHIMYQRQQ LPLPYEQLKH FYRKPSPQAE EMLKKKPRAT TEVSSRKCQQ ALAELESVLS HLEDFFARTL VPRVLILLGG NALSPKEFYE LDLSLLAPYS VDQSLSTAAC LRRLFRAIFM ADAFSELQAP PLMGTVVMAQ GHRNCGEDWF RPKLNYRVPS RGHKLTVTLS CGRPSIRTTA WEDYIWFQAP VTFKGFRE
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Molecular Weight
34 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
MAD2L1BP, also known as MAD2-Like 1 Binding Protein, is a crucial component involved in the mitotic spindle assembly checkpoint, which ensures the proper segregation of chromosomes during cell division. Its role in the cell cycle has garnered significant interest, particularly in the context of cancer research, as dysregulation of this checkpoint can lead to aneuploidy and tumorigenesis. Recent studies have indicated that MAD2L1BP interacts with various proteins involved in this checkpoint pathway, emphasizing its importance in maintaining genomic stability. Moreover, MAD2L1BP has been implicated in cellular responses to DNA damage, further underlining its potential as a biomarker for tumor progression. The recombinant protein form of MAD2L1BP allows researchers to investigate its structure-function relationships and interactions in vitro, paving the way for therapeutic innovations. Understanding the dynamics of MAD2L1BP could reveal novel strategies for targeting cancer cells that exploit defective mitotic regulation, paving the way for potential therapeutic interventions aimed at enhancing the effectiveness of existing treatments or developing new targeted therapies. The ongoing exploration of MAD2L1BP and its molecular mechanisms continues to contribute to the broader understanding of cell cycle regulation and its implications in oncogenesis.
