Recombinant Human Serine/Arginine-Rich Splicing Factor 9 (SRSF9) Protein (GST)

Name: Recombinant Human Serine/Arginine-Rich Splicing Factor 9 (SRSF9) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-10302P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Serine/Arginine-Rich Splicing Factor 9 (SRSF9) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13242
Target Symbol	SRSF9
Synonyms	arginine/serine-rich 9; Pre mRNA splicing factor SRp30C; Pre-mRNA-splicing factor SRp30C; Serine/arginine-rich splicing factor 9; SFRS 9; Splicing factor; Splicing factor arginine/serine rich 9; splicing factor, arginine/serine-rich 9; splicing factor, arginine/serine-rich, 30-KD, C; SR splicing factor 9; SRP30C; SRSF9; SRSF9_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
Expression Range	1-221aa
Protein Length	Full Length
Mol. Weight	52.5kDa
Research Area	Transcription
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10.
Subcellular Location	Nucleus. Note=Cellular stresses such as heat shock may induce localization to discrete nuclear bodies termed SAM68 nuclear bodies (SNBs), HAP bodies, or stress bodies. Numerous splicing factors including SRSF1/SFRS1/SF2, SRSF7/SFRS7, SAFB and KHDRBS1/SAM68 accumulate at these structures, which may participate in the post-transcriptional regulation of mRNAs in stressed cells.
Protein Families	Splicing factor SR family
Database References	HGNC: 10791 OMIM: 601943 KEGG: hsa:8683 STRING: 9606.ENSP00000229390 UniGene: Hs.706889
Tissue Specificity	Expressed at high levels in the heart, kidney, pancreas and placenta, and at lower levels in the brain, liver, lung and skeletal muscle.

Gene Functions References

Dehydroepiandrosterone (DHEA) and cortisol modulate SRSF9 and SRSF3 in a different way and data suggest that the anti-glucocorticoid effect of DHEA, among other mechanisms, is also exerted by modulating the expression of proteins involved in the splicing of the GR pre-mRNA. PMID: 28373129
Report no correlation between expression of glucocorticoid receptor isoforms and SRp30c. PMID: 25665148
Overexpression of SRSF9 and SRSF1 promote beta-catenin accumulation via the recruitment of beta-catenin mRNA and by enhancing its translation in an mTOR-dependent manner. PMID: 23592547
Relative levels of SRp20, SRp30c, and SRp40 in TM cells control differential expression of the two alternatively spliced isoforms of the GR and thereby regulate GC responsiveness. PMID: 22205602
these data indicated that tumor suppressive miR-1 induces apoptosis through direct inhibition of SRSF9 in bladder cancer. PMID: 22178073
These results suggest that SRp30c can activate human papillomavirus type 16 L1 mRNA expression via a bimodal mechanism: directly by stimulating splicing to late splice sites and indirectly by inhibiting competing early splice sites. PMID: 21697349
SRp30c can function as a repressor of 3' splice site utilization and suggest that the SRp30c-CE9 interaction may contribute to the control of hnRNP A1 alternative splicing. PMID: 12024014
SRp30c protein is an interacting protein of YB-1 PMID: 12604611
Serine-arginine-rich protein p30 directs alternative splicing of glucocorticoid receptor pre-mRNA to glucocorticoid receptor beta in neutrophils. PMID: 12738786
Results suggest that bombesin-induced expression of SRp30c affects gllucorticoid receptor (GR) pre-mRNA splicing, leading to increased GR beta expression and contributing to glucocorticoid resistance in PC cells. PMID: 17540466
Study shows that PTB can function as an anti-repressor molecule to counteract the splicing inhibitory activity of SRp30c. PMID: 17548433
SRp30c stimulates splicing to the downstream 5' splice site of Bcl-x(L), thereby attenuating the repressive effect of upstream U1 snRNP binding sit PMID: 18534987
findings indicate the importance of arginine methylation for the subnuclear localization of SFRS9. PMID: 19557313

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.