Recombinant Proteins

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SNRPA1 Human

Small Nuclear Ribonucleoprotein Polypeptide A1 Human Recombinant

Recombinant human SNRPA1 is produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 275 amino acids (1-255 a.a.) with a molecular weight of 30.5kDa. The protein has a 20 amino acid His-tag fused at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT558
Source
Escherichia Coli.
Appearance
A clear, sterile filtered solution.

SNRPB Human

Small Nuclear Ribonucleoprotein Polypeptides B & B1 Human Recombinant

Recombinant human SNRPB, produced in SF9 cells, is a glycosylated polypeptide with a predicted molecular weight of 25.4 kDa. On SDS-PAGE, it migrates at approximately 30 kDa. The protein is expressed with a 6x His tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT637
Source
Sf9 insect cells.
Appearance
Clear, sterile-filtered solution.

SNRPB2 Human

Small Nuclear Ribonucleoprotein Polypeptide B Human Recombinant

Recombinant human SNRPB2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein, fused with a 20 amino acid His tag at its N-terminus, comprises 245 amino acids (1-225a.a.) and has a molecular weight of 27.6kDa. Purification of SNRPB2 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT708
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

SNRPD2 Human

Small Nuclear Ribonucleoprotein Polypeptide D2 Human Recombinant

This product consists of recombinant human SNRPD2 protein with a 20 amino acid His tag fused at its N-terminus. Produced in E. coli, it exists as a single, non-glycosylated polypeptide chain with a molecular weight of 15.6 kDa. The protein encompasses 138 amino acids, including the 118 amino acids of SNRPD2 (1-118 a.a.). Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1137
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

SNRPD2 Human, Sf9

Small Nuclear Ribonucleoprotein Polypeptide D2 Human Recombinant, Sf9

Recombinant human SNRPD2, expressed in SF9 insect cells, is a glycosylated polypeptide chain with a calculated molecular mass of 14.773 kDa. It is engineered with a 6x His tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1212
Source
Sf9 insect cells.
Appearance
Clear, sterile-filtered solution.

SNRPD3 Human

Small Nuclear Ribonucleoprotein Polypeptide D3 Human Recombinant

Recombinant SNRPD3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 146 amino acids (residues 1-126). It has a molecular weight of 16.0 kDa. For purification purposes, a 20 amino acid His-Tag is fused to the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1343
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

SNRPD3 Human, Sf9

Small Nuclear Ribonucleoprotein Polypeptide D3 Human Recombinant, Sf9

Recombinantly produced in SF9 cells, SNRPD3 Human is a glycosylated polypeptide chain with a calculated molecular mass of 14,739 Daltons. 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.
BT1455
Source
Sf9 insect cells.
Appearance
Clear, sterile-filtered solution.

Sm Bovine

Bovine Small Nuclear Ribonucleoprotein Polypeptide

Small Nuclear Ribonucleoprotein Polypeptides, derived from bovine tissues, have been purified using proprietary protein-chemical methods.
Shipped with Ice Packs
Cat. No.
BT228
Source
Bovine tissues.
Appearance
A clear solution that has undergone sterile filtration.

SNRNP25 Human

Small Nuclear Ribonucleoprotein 25kDa Human Recombinant

Produced in E. coli, SNRNP25 is a single, non-glycosylated polypeptide chain consisting of 152 amino acids (1-132 a.a.) with a molecular weight of 17.4 kDa. It includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT305
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

SNRNP70 Human

Small Nuclear Ribonucleoprotein 70kDa Human Recombinant

Recombinant Human U1-snRNP 68kDa cDNA encodes for the 70kDa isoform of the human U1-snRNP 68 protein. This isoform lacks 66 internal amino acids outside the known epitope-containing areas. It is fused to a hexahistidine purification tag and has a calculated molecular weight of 68.0 kDa.
Shipped with Ice Packs
Cat. No.
BT389
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.
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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