SNRPC Human

Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant
Cat. No.
BT771
Source
Escherichia Coli.
Synonyms
U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

SNRPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a.) and having a molecular mass of 19.8kDa (Molecular weight on SDS-PAGE will appear higher).
SNRPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
SNRPC, part of the U1 small nuclear ribonucleoprotein C family, is crucial for spliceosome formation. This protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle is involved in nuclear precursor messenger RNA splicing. Autoantibodies, often found in patients with connective tissue diseases, target snRNP particles.
Description
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.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The SNRPC protein solution (0.25 mg/ml) is supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 50% glycerol, 0.3 M NaCl, 5 mM DTT, and 2 mM EDTA.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze the product at -20°C. It is advisable to add a carrier protein (0.1% HSA or BSA) for long-term storage. To maintain product integrity, avoid repeated freezing and thawing.
Purity
Purity is determined to be greater than 85% using SDS-PAGE analysis.
Synonyms
U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKFYCD YCDTYLTHDS PSVRKTHCSG RKHKENVKDY YQKWMEEQAQ SLIDKTTAAF QQGKIPPTPF SAPPPAGAMI PPPPSLPGPP RPGMMPAPHM GGPPMMPMMG PPPPGMMPVG PAPGMRPPMG GHMPMMPGPP MMRPPARPMM VPTRPGMTRP DR.

Product Science Overview

Gene and Protein Structure

The SNRPC gene is located on human chromosome 6p21.31 . It encodes a protein that is a specific component of the U1 snRNP particle. The U1 snRNP is one of the first snRNPs to interact with pre-mRNA, recognizing the 5’ splice site and facilitating the assembly of the spliceosome . The spliceosome is a complex molecular machine responsible for removing introns from pre-mRNA and ligating exons together.

Function and Mechanism

SNRPC is directly involved in the initial recognition of the 5’ splice site of pre-mRNA. This recognition is crucial for both constitutive and regulated alternative splicing . The interaction between SNRPC and the 5’ splice site precedes the base-pairing between the pre-mRNA and the U1 snRNA, ensuring accurate splicing and processing of mRNA .

Clinical Significance

SNRPC is not only essential for normal cellular function but also has clinical significance. Autoantibodies targeting snRNP particles, including SNRPC, are frequently produced by patients with connective tissue diseases . These autoantibodies can interfere with the normal function of snRNPs, leading to defects in mRNA splicing and contributing to disease pathology.

Research and Applications

Recombinant human SNRPC is used in various research applications to study the mechanisms of RNA splicing and the role of snRNPs in cellular processes. Understanding the function and regulation of SNRPC can provide insights into the molecular basis of diseases associated with splicing defects and aid in the development of therapeutic strategies.

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