Alternative Name(s):

Pre-mRNA-splicing factor SRp30CSplicing factor, arginine/serine-rich 9

Species: (Organism)

Homo sapiens (Human)

Gene Names:

SRSF9

Tag info:

N-terminal GST-tagged

Target Protein AA Sequence:

MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY

Expression Region:

1-221aa

Subcellular Location:

Nucleus

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.

Protein Length:

Full Length

Pathway:

Mol. Weight:

52.5 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Transcription

Function:

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10.

Involvement in disease:

Relevance:

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Splicing factor SR family

Reference:

Identification and characterization of three members of the human SR family of pre-mRNA splicing factors.Screaton G.R., Caceres J.F., Mayeda A., Bell M.V., Plebanski M., Jackson D.G., Bell J.I., Krainer A.R.EMBO J. 14:4336-4349(1995)