Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

LSM1 Human

LSM1 Homolog, U6 Small Nuclear RNA Associated Human Recombinant

LSM1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (1-133 a.a.) and having a molecular mass of 17.3kDa. The LSM1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20452
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LSM12 Human

LSM12 Homolog, U6 Small Nuclear RNA Associated Human Recombinant

LSM12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-195 a.a.) and having a molecular mass of 24.1kDa.
LSM12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20563
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

LSM2 Human

LSM2 Homolog, U6 Small Nuclear RNA Associated Human Recombinant

LSM2 Human Recombinant produced in E. coli is a single polypeptide chain containing 119 amino acids (1-95) and having a molecular mass of 13.4kDa.
LSM2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20649
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

LSM3 Human

LSM3 Homolog, U6 Small Nuclear RNA Associated Human Recombinant

LSM3 Human Recombinant produced in E. coli is a single polypeptide chain containing 125 amino acids (1-102) and having a molecular mass of 14.3kDa.
LSM3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20698
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

LSM4 Human

LSM4 Homolog, U6 Small Nuclear RNA Associated Human Recombinant

LSM4 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids (1-139 a.a.) and having a molecular mass of 17.5kDa. The LSM4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20792
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

LSM5 Human

LSM5 Homolog, U6 Small Nuclear RNA Associated Human Recombinant

LSM5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (1-91 a.a) and having a molecular mass of 12.3kDa.
LSM5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20880
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
Definition and Classification

U6 small nuclear RNA (snRNA) is a non-coding RNA component of the spliceosome, a complex responsible for the removal of introns from pre-mRNA . It is one of the five uridine-rich snRNAs (U1, U2, U4, U5, and U6) that are essential for the splicing process . U6 snRNA is transcribed by RNA polymerase III and is characterized by its high uridine content .

Biological Properties

Key Biological Properties: U6 snRNA is highly conserved across species and forms a crucial part of the spliceosome’s catalytic core . It is metabolically stable and synthesized by RNA polymerase III .

Expression Patterns and Tissue Distribution: U6 snRNA is ubiquitously expressed in eukaryotic cells and is confined to the nucleus, specifically within the splicing speckles and Cajal bodies . It is present in multiple copies throughout the genome, with some copies being pseudogenes .

Biological Functions

Primary Biological Functions: U6 snRNA plays a pivotal role in the splicing of pre-mRNA by forming the catalytic core of the spliceosome . It interacts with other snRNAs (U2, U4, and U5) and various proteins to facilitate the precise removal of introns .

Role in Immune Responses and Pathogen Recognition: While U6 snRNA’s primary function is in RNA splicing, its involvement in immune responses and pathogen recognition is not well-documented. However, the proper functioning of the spliceosome is crucial for the expression of immune-related genes .

Modes of Action

Mechanisms with Other Molecules and Cells: U6 snRNA interacts with U4 snRNA to form a stable complex, which is later unwound to allow U6 to pair with U2 snRNA . This interaction is essential for the catalytic activity of the spliceosome .

Binding Partners and Downstream Signaling Cascades: U6 snRNA binds to several proteins, including LSm proteins and other snRNP-specific proteins, to form the U6 snRNP complex . This complex coordinates the magnesium ions required for the splicing reaction and positions the substrate for catalysis .

Regulatory Mechanisms

Transcriptional Regulation: U6 snRNA is transcribed by RNA polymerase III, and its promoter contains several regulatory elements, including the proximal sequence element (PSE), octamer element (OCT), and TATA box . These elements are crucial for the efficient transcription of U6 snRNA .

Post-Translational Modifications: U6 snRNA undergoes several modifications, including 2’-O-methylation and pseudouridylation, which are essential for its stability and function .

Applications

Biomedical Research: U6 snRNA is widely used as a reference gene in gene expression studies due to its stable expression . It is also employed in RNA interference (RNAi) and CRISPR/Cas9 systems for gene knockdown and genome editing .

Diagnostic Tools and Therapeutic Strategies: U6 snRNA’s involvement in splicing makes it a potential target for therapeutic interventions in diseases caused by splicing defects . Its stable expression also makes it a reliable marker in diagnostic assays .

Role in the Life Cycle

Development to Aging and Disease: U6 snRNA is essential throughout the life cycle, from development to aging . Its role in splicing is crucial for the proper expression of genes involved in various biological processes. Defects in U6 snRNA or its associated proteins can lead to splicing errors, contributing to diseases such as cancer and neurodegenerative disorders .

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