Recombinant Proteins

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SNRPA Human

Small Nuclear Ribonucleoprotein Polypeptide A Human Recombinant

Recombinant SNRPA Human protein, expressed in SF9 cells, is a glycosylated polypeptide with a molecular weight of 34 kDa. This protein is engineered with a -6x His tag at the N-terminus to facilitate purification. It is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT459
Source
Sf9 insect cells.
Appearance
Clear, sterile solution after filtration.

SNRPE Human

Small Nuclear Ribonucleoprotein Polypeptide E Human Recombinant

This product consists of the human recombinant SNRPE protein, fused with a 20 amino acid His tag at its N-terminus. It is produced in E.Coli and is a single, non-glycosylated polypeptide chain. The protein comprises 112 amino acids (specifically, amino acids 1 to 92 of the SNRPE sequence) and has a molecular weight of 12.9kDa. Purification of SNRPE is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1576
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution.

SNRPF Human

Small Nuclear Ribonucleoprotein Polypeptide F Human Recombinant

This product consists of a single, non-glycosylated polypeptide chain of SNRPF, produced in E. coli. It encompasses amino acids 1-86a.a., resulting in a molecular weight of 11.8 kDa. For purification and detection purposes, a 20 amino acid His-tag is fused to the N-terminus. The protein has undergone purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1670
Source
Escherichia Coli.
Appearance
The product appears as a clear solution that has been sterilized through filtration.

SNRPG Human

Small Nuclear Ribonucleoprotein Polypeptide G Human Recombinant

Recombinant human SNRPG, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein comprises 96 amino acids (including a 20 amino acid His tag at the N-terminus, spanning residues 1-76) and has a molecular weight of 10.6 kDa. Purification of SNRPG is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT1740
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

SNRPC Human

Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant

Recombinant human SNRPC, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 182 amino acids (1-159 a.a.), including a 23 amino acid His-tag at the N-terminus, and has a molecular mass of 19.8 kDa. Note that the molecular weight on SDS-PAGE will appear higher. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT771
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

SNRPC Human, Sf9

Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant, Sf9

Recombinant Human SNRPC, produced in Sf9 cells, is a glycosylated polypeptide chain with a molecular weight of 25 kDa. It is expressed with a C-terminal 6x His tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT872
Source
Sf9 insect cells.
Appearance
Clear, sterile, filtered solution.

SNRPD Human

Small Nuclear Ribonucleoprotein Polypeptide D1, D2, D3 Human Recombinant

SNRPD Human Recombinant, produced in SF9 insect cells, is a mixed protein complex comprising the SNRPD1 (14,306 Dalton), SNRPD2 (14,773 Dalton), and SNRPD3 (14,739 Dalton) proteins. Each protein (SNRPD1, SNRPD2, and SNRPD3) is individually tagged with a 6xHis tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT942
Source
Sf9 insect cells.
Appearance
Clear, sterile-filtered solution.

SNRPD1 Human

Small Nuclear Ribonucleoprotein Polypeptide D1 Human Recombinant

SNRPD1 Human Recombinant, produced in SF9, is a glycosylated polypeptide chain with a calculated molecular mass of 16kDa. This protein is expressed with a -6x His tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1057
Source
Sf9 insect cells.
Appearance
Sterile Filtered clear solution.

Nucleosome Bovine

Bovine Nucleosome

Nucleosome Bovine, purified from bovine tissues using proprietary protein-chemical techniques, exhibits multiple bands in the molecular weight range of 14-18 kDa on SDS-PAGE analysis.
Shipped with Ice Packs
Cat. No.
BT29056
Source

Bovine tissues.

Appearance
Sterile Filtered clear solution.

RNP/Sm Bovine

Bovine RNP/Sm Ribonucleoprotein Complex

RNP/Sm Bovine is isolated from bovine tissues using proprietary protein purification methods.

Shipped with Ice Packs
Cat. No.
BT29126
Source

Bovine tissues.

Appearance
A clear solution that has been sterilized by filtration.
Definition and Classification

Small nuclear ribonucleoproteins (snRNPs), often pronounced as “snurps,” are RNA-protein complexes that play a crucial role in the splicing of pre-messenger RNA (pre-mRNA) in eukaryotic cells . They are essential components of the spliceosome, a large RNA-protein molecular complex responsible for removing introns from pre-mRNA . There are several types of snRNPs, each containing a specific small nuclear RNA (snRNA) and associated proteins. The major snRNPs involved in splicing are U1, U2, U4, U5, and U6 . Additionally, there are variant snRNPs such as U11, U12, U4atac, and U6atac, which are involved in the splicing of a specific class of introns .

Biological Properties

snRNPs exhibit key biological properties, including their specific expression patterns and tissue distribution. They are predominantly found in the nucleus of eukaryotic cells, where they participate in the splicing of pre-mRNA . The snRNA component of snRNPs is typically about 150 nucleotides in length and plays a critical role in recognizing splicing signals at the 5’ and 3’ ends of introns . The expression of snRNPs can vary across different tissues, with certain snRNPs being more abundant in specific cell types .

Biological Functions

The primary biological function of snRNPs is to facilitate the splicing of pre-mRNA by forming the spliceosome . This process is essential for the removal of introns and the joining of exons to produce mature mRNA, which can then be translated into proteins . snRNPs also play a role in immune responses and pathogen recognition. For example, certain snRNPs have been implicated in the regulation of immune signaling pathways and the recognition of viral RNA .

Modes of Action

snRNPs interact with other molecules and cells through various mechanisms. They bind to specific sequences within pre-mRNA to recognize and catalyze the splicing process . The snRNA component of snRNPs provides the specificity for binding to critical splicing signals, while the protein components facilitate the assembly and activation of the spliceosome . Additionally, snRNPs can interact with other splicing factors and regulatory proteins to modulate the splicing process .

Regulatory Mechanisms

The expression and activity of snRNPs are tightly regulated through multiple mechanisms. Transcriptional regulation of snRNA genes is controlled by specific transcription factors and promoter elements . Post-transcriptional modifications, such as methylation and pseudouridylation, also play a role in the maturation and function of snRNAs . Furthermore, the assembly of snRNPs involves the coordinated synthesis and transport of snRNA and protein components between the nucleus and cytoplasm .

Applications

snRNPs have several applications in biomedical research, diagnostic tools, and therapeutic strategies. They are used as markers for studying RNA splicing and gene expression regulation . In diagnostic tools, snRNPs can serve as biomarkers for certain diseases, such as autoimmune disorders and cancers . Therapeutically, targeting snRNPs and their associated splicing machinery has potential in treating diseases caused by splicing defects .

Role in the Life Cycle

snRNPs play a critical role throughout the life cycle, from development to aging and disease. During development, snRNPs are involved in the regulation of gene expression and the production of proteins necessary for cell differentiation and growth . In aging, changes in snRNP function and splicing efficiency can contribute to age-related diseases and cellular senescence . Additionally, snRNPs are implicated in various diseases, including cancer, where they can influence tumor progression and response to therapy .

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