HNRNPK Human
Heterogeneous Nuclear Ribonucleoprotein K Human Recombinant
Cat. No.
BT20802
Source
Escherichia Coli.
Synonyms
CSBP, HNRPK, TUNP, Heterogeneous nuclear ribonucleoprotein K, hnRNP K, Transformation up-regulated nuclear protein, HNRNPK.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
HNRNPK Human Recombinant produced in E. coli is a single polypeptide chain containing 299 amino acids (1-276) and having a molecular mass of 33kDa. HNRNPK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Heterogeneous Nuclear Ribonucleoprotein K, also called HNRNPK, belongs to a family of proteins known as heterogeneous nuclear ribonucleoproteins (hnRNPs) found throughout the body. HNRNPK plays a role in the response of the p53/TP53 pathway to DNA damage, acting on both the activation and suppression of gene transcription. Primarily located in the nucleoplasm, HNRNPK contains three KH domains that enable it to bind to RNA molecules.
Description
Recombinant human HNRNPK, produced in E. coli, is a single chain polypeptide comprising 299 amino acids (specifically residues 1 to 276) and exhibiting a molecular weight of 33kDa. The protein includes a 23 amino acid His-tag fused at its N-terminus. Its purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear solution that has undergone sterile filtration.
Formulation
The HNRNPK solution (provided at a concentration of 1mg/ml) contains 20mM Tris-HCl buffer with a pH of 8.0, 0.15M NaCl, 20% glycerol, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the solution should be kept refrigerated at 4°C. For extended storage, it is recommended to store the solution frozen at -20°C. Adding a carrier protein (either 0.1% HSA or BSA) is advisable for long-term storage. It's important to avoid repeatedly freezing and thawing the solution.
Purity
The purity level is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
CSBP, HNRPK, TUNP, Heterogeneous nuclear ribonucleoprotein K, hnRNP K, Transformation up-regulated nuclear protein, HNRNPK.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMETEQPE ETFPNTETNG EFGKRPAEDM EEEQAFKRSR NTDEMVELRI LLQSKNAGAV IGKGGKNIKA LRTDYNASVS VPDSSGPERI LSISADIETI GEILKKIIPT LEEGLQLPSP TATSQLPLES DAVECLNYQH YKGSDFDCEL RLLIHQSLAG GIIGVKGAKI KELRENTQTT IKLFQECCPH STDRVVLIGG KPDRVVECIK IILDLISESP IKGRAQPYDP NFYDETYDYG GFTMMFDDRR GRPVGFPMRG RGGFDRMPPG RGGRPMPPS.
Product Science Overview
Structure and Function
HNRNPK contains three unique structural motifs known as KH domains, which are responsible for binding to poly© DNA and RNA sequences . These domains enable HNRNPK to interact with various nucleic acids, making it a versatile player in RNA metabolism. The protein is predominantly located in the nucleoplasm but can shuttle between the nucleus and the cytoplasm .
Biological Roles
HNRNPK is involved in several critical cellular processes, including:
- Pre-mRNA Processing: HNRNPK binds to pre-mRNA as part of heterogeneous ribonucleoprotein particles, influencing the splicing and maturation of mRNA .
- Transcription Regulation: It acts as a transcription activator and repressor, particularly in response to DNA damage through the p53/TP53 pathway .
- Signal Transduction: HNRNPK is implicated in various signaling pathways, contributing to cellular responses to external stimuli .
- Cell Cycle Progression: The protein plays a role in the regulation of the cell cycle, ensuring proper cell division and proliferation .
Clinical Significance
Recombinant HNRNPK
Recombinant HNRNPK refers to the protein produced through recombinant DNA technology, which involves inserting the HNRNPK gene into an expression system to produce the protein in vitro. This recombinant protein is used in research to study its structure, function, and role in diseases, as well as in the development of potential therapeutic interventions .
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