SRSF2 Antibodies

Serine/arginine-rich splicing factor 2 (SRSF2)

Necessary for the splicing of pre-mRNA.

It is needed for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly.

It also is needed for ATP-dependent interactions of both U1 and U2 snRNPs with pre- mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding elements, U1 snRNP and U2AF.

Gene Information

Human
Gene Name:	SRSF2
Uniprot:	Q01130
Entrez:	6427

Family

Belongs to:
splicing factor SR family

Alternative Names

PR264; SC35; SC-35; serine/arginine-rich splicing factor 2; SFRS2; SFRS2A; splicing component, 35 kDa; splicing factor SC35; splicing factor, arginine/serine-rich 2; SR splicing factor 2; SRp30b

Molecular Weight

Mass (kDA):
25.476 kDA

Genomic Context

Human
Location:	17q25.1
Sequence:	17; NC_000017.11 (76734115..76737411, complement)

Subcellular Localizations

Nucleus. Nucleus, nucleoplasm. Nucleus speckle. Phosphorylation by SRPK2 provokes its redistribution from the nuclear specke to nucleoplasm.

Diseases

• Leukemia
• Neoplasms
• Hiv Infections
• Dysmyelopoietic Syndromes
• Immunologic Deficiency Syndromes
• Malignant Neoplasms
• Myeloid Leukemia
• Myelomonocytic Leukemia
• Leukemia, Myelocytic, Acute
• Cell Transformation, Neoplastic
• Leukemia, Myelomonocytic, Chronic
• Neurodegenerative Disorders

• Alzheimer's Disease
• Carcinoma
• Hematologic Neoplasms
• Juvenile Myelomonocytic Leukemia
• Tauopathies
• Muscular Atrophy

Interacting Proteins

• CIR1
• KAT5
• SNRNP70
• U2AF1

Pathways

• Localization
• Transport
• Cell Cycle
• Pathogenesis
• Mitosis
• Rna Splicing
• Interphase
• Mrna Splicing
• Rna Processing
• Nuclear Export
• Nuclear Import
• Cell Death
• Cell Proliferation

• Telophase
• Translation
• Cell Division
• Embryo Implantation
• Dna Repair
• Regeneration
• Cellular Localization

PTMs

• Phosphorylation
• Cleavage
• Methylation
• Acetylation

• Dephosphorylation
• Demethylation
• Prenylation
• Ubiquitination

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SRSF2

Writing a Steven Boster Bio - Best Uses of the SRSF2 Marker

You have just written a Steven Boster bio. But how can you optimize it? Using the SRSF2 marker can help you achieve this goal. This article will provide background information and tips on how to optimize your SRSF2 experiment. We'll also talk about the importance of using highly concentrated antibodies. The best methods of sample preparation will be discussed.

Using SRSF2 markers

SRSF2 plays a critical role in the progression of gliomas. This protein is upregulated in gliomas. We used a CFSE stain in this study to measure cell growth. We found that SRSF2 mutated cells didn't cause cell proliferation, but they increased apoptosis. This is consistent with previous observations that mutant SRSF2 has a high association with apoptosis.

The Serine-arginine rich splicing factors 2 (SRSF2) protein is well-known for its role in RNA splicing, and genome stability. It is frequently mutated in patients with MDS, with the most common mutation occurring at proline 95. Mutated proteins have different RNA binding preferences and may influence splicing. However, it is not clear what role SRSF2 mutations play in MDS.

SRSF2 is usually located in the nucleus. However mutations in this protein may alter its cellular position. Anti-HA antibodies stained tet cells and revealed that SRSF2WT (and SRSF2P95H) were primarily located in the nucleus. SRSF2P95R, SRSF2DRRM and SRSF2WT were found in the cytoplasm. The deletion of NRS allows SRSF2 shuttle between the nucleus & cytoplasm.

About 10% of patients with myelodysplastic disease and 25-30% with chronic myelomonocyticleukemia have SRSF2 mutations. These disorders are common in older people, with a high rate of incidence among those over sixty. This is the only treatment that is effective for these patients. However, it is often not possible due either to advanced disease or patient age.

MDS-related SRSF2 mutants are similar to wild type SRSF2 in many aspects. They phosphorylate SRSF2 and splice select alternative splicing events. The P95 point mutant in SRSF2 causes the same alternative splicing change without the conventional DDR. These findings could indicate the importance of SRSF2 in determining cell fate after damage to DNA.

History of Steven Boster

A quick internet search of Steven Boster’s public records will give you details on his current, past, and known relatives, aswell as mobile phone numbers. His long and distinguished history has made him the subject of numerous books and television programs. He was a passionate sports fan, especially the games of the opposing team. He was also an avid fan of auto racing, never missing Friday night action at the local track. He also attended extra events, including dirt-track races.

Steve Boster died on June 6, 2022. He was born Joliet in Illinois. He was a veteran of U.S. Army, having worked in retail sales for many decades. He was also a member of Concordia Hall in Staunton, VA. His family members include his two Daughters, Natosha Peck and Crystal Boster, six grandchildren, and four brothers, Jack and Sandra Blanton. His nieces and nephews also survived him.