CUL1 Human

Cullin-1 Human Recombinant
Cat. No.
BT3389
Source
Escherichia Coli.
Synonyms
Cullin 1, CUL-1, Cullin-1
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTeks 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.
Shipped with Ice Packs
In Stock

Description

CUL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 430 amino acids (1- 410a.a.) and having a molecular mass of 49.4kDa.
CUL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cullin1 is a crucial part of various cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. These complexes help ubiquitinate proteins involved in cell cycle progression, signal transduction, and transcription. Within the SCF complex, Cullin1 acts as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. It contributes to catalysis by positioning the substrate and the ubiquitin-conjugating enzyme.
Description
CUL1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 430 amino acids (1-410 a.a.) with a molecular weight of 49.4 kDa. It features a 20 amino acid His-tag fused at the N-terminus and is purified through proprietary chromatographic techniques.
Physical Appearance
Clear, sterile filtered solution.
Formulation
The CUL1 protein solution (1mg/ml) is prepared in a 20mM Tris-HCl buffer with a pH of 8.0, containing 1mM DTT, 100mM NaCl, and 10% glycerol.
Purity
Purity exceeds 95%, as determined by SDS-PAGE analysis.
Stability
For use within 2-4 weeks, store at 4°C. For long-term storage, freeze at -20°C. Avoid repeated freeze-thaw cycles.
Synonyms
Cullin 1, CUL-1, Cullin-1
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK

Product Science Overview

Structure and Function

Cullin-1 serves as a scaffold protein within the SCF complex. It organizes the SKP1-F-box protein and RBX1 subunits, facilitating the ubiquitination process. The SCF complex’s E3 ubiquitin ligase activity is dependent on the neddylation of the cullin subunit, although this may be dispensable for some in vitro reactions .

Recombinant Production

Recombinant human Cullin-1 is typically produced in various expression systems, including Escherichia coli (E. coli), Spodoptera frugiperda (Sf 21) cells, and wheat germ . The recombinant protein is often tagged with His-tag for purification purposes and is available in different formulations, such as carrier-free or with Bovine Serum Albumin (BSA) to enhance stability .

Applications

Recombinant Cullin-1 is used in various research applications, including:

  • In vitro ubiquitination assays: To study the ubiquitination process and identify potential substrates.
  • Protein-protein interaction studies: To investigate interactions within the SCF complex and with other cellular proteins.
  • Structural biology: To determine the structure of the SCF complex and understand its mechanism of action.
Storage and Stability

Recombinant Cullin-1 is typically supplied as a solution in buffers containing HEPES, NaCl, DTT, and glycerol. It is shipped with dry ice and should be stored at -70°C to maintain stability. Repeated freeze-thaw cycles should be avoided to preserve protein integrity .

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