Analytical Data
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Gene name
CRSP9
- Application
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Alternative Names
Activator recruited cofactor 34 kDa component; Activator-recruited cofactor 34 kDa component; ARC34; Cofactor required for Sp1 transcriptional activation subunit 9; Cofactor required for Sp1 transcriptional activation; subunit 9 (33kD); Cofactor required for Sp1 transcriptional activation; subunit 9; 33kDa; CRSP complex subunit 9; CRSP33
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43513
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Expression Region
1-233aa
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AA Sequence
MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKTEPMDADDSNNCTGQNEHQRENSGHRRDQIIEKDAALCVLIDEMNERP
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Molecular Weight
51.37 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
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Protein Description
CRSP9, short for Coactivator Required for Splicing 9, is a pivotal protein that plays a multifaceted role in various cellular processes, particularly in gene expression and RNA splicing. Research has revealed that CRSP9 is a crucial component of the CRSP complex, which interacts with RNA polymerase II and is involved in the transcriptional regulation of a wide array of genes. The protein's functional significance has attracted considerable attention in the context of cancer biology, as its dysregulation is often associated with tumorigenesis. Furthermore, CRSP9 is implicated in the modulation of alternative splicing, a process that can generate diverse protein isoforms from a single gene, thus influencing cellular functionality and adaptability. Given its central role in these fundamental biological processes, understanding the mechanisms governing CRSP9's function, including its interactions with other splicing factors and transcriptional coactivators, is crucial for unraveling the complexities of gene regulation. Recent advancements in structural biology and proteomics have facilitated a deeper exploration of CRSP9's interactions and regulatory mechanisms, providing insights that could lead to potential therapeutic strategies targeting its dysregulation in various diseases.
