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• Healthcare & Medical (primary)

Products

• Dr. Gold's Bacterial Protein Extraction Reagent — Enhanced Performance | Greater Yields | Cost-Effective Dr. Gold’s Bacterial Protein Extraction Reagent is a powerful, next-generation solution designed for efficient extraction of expressed proteins from bacterial cells—now reengineered for improved performance and cost-effectiveness. Built on the foundation of our trusted Bacterial Cell Lysis Buffer, this ready-to-use formulation offers enhanced yield and reproducibility without the need for harsh mechanical disruption. Our proprietary blend of buffering agents and dialyzable, non-denaturing detergents ensures gentle but thorough lysis, preserving native protein structure and activity. The reagent includes lysozyme, nucleases, and a specially optimized salt solution to promote full membrane disruption and maximize the recovery of soluble proteins. Whether you're preparing samples for SDS-PAGE, purification, or enzymatic assays, Dr. Gold’s reagent offers superior protein extraction with consistent, repeatable results—batch after batch. Key Features Ready-to-use formulation—no additional components required Contains both non-ionic and zwitterionic detergents in Tris buffer Includes lysozyme and nucleases for complete cell breakdown Enhanced salt formulation improves soluble protein recovery Compatible with common reducing agents and protease inhibitors Suitable for use with both fresh and frozen bacterial pellets Outperforms leading competitors in soluble protein yield and clarity Kit Component Dr. Gold’s Bacterial Protein Extraction Reagent GB Enzyme Mix Salt Solution Note: The Salt Solution is not strictly required for lysis, but our research has shown it significantly enhances protein solubility and yield. Storage/Handling This product may be shipped with blue ice. Dr. Gold’s Bacterial Protein Extraction Reagent and Salt Solution should be stored at 4°C, GB Enzyme Mix should be stored at -20°C immediately upon arrival. When stored under the recommended conditions and handled correctly, these products should be stable for at least 1 year from the date of receipt. FAQ How much reagent do I need to use with my culture? Use 1.3 mL of extraction buffer per 10 mL of culture at A600 = 2.0. Adjust proportionally for different cell densities and volumes. Does the reagent contain EDTA or other chelating agents? is the reagent compatible with metal affinity chromatography (His tagged proteins)? No! Dr. Gold’s Bacterial Protein Extraction Reagent does not contain EDTA or other chelating agents. It is fully compatible with His-Tag affinity chromatography. Can proteins isolated using Dr. Gold’s Bacterial Protein Extraction Reagent be quantified using Bradford or BCA or will there be background due to lysozyme and nucleases? There may be some background signal from the added enzymes, but in our testing it's not enough to skew the total extraction results (Levels are undetectable on SDS-Page Gels of extracted material).
• IPTG — IPTG is an analog of galactose that is non-metabolizable and inactivates the lac repressor to induce synthesis of β-galactosidase in E. coli. The expression of cloned genes under the control of the lac operon is induced by IPTG. It is also a substrate for thigalactoside transacetylase and has been reported to induce penicillinase in bacteria. IPTG is commonly used in cloning procedures that require induction of β-galactosidase and is most often used with X-Gal (Gold Bio #X4281C) or Bluo-Gal (Gold Bio #B-673) for blue/white colony screening or Magenta-Gal (Gold Bio #B-378) for red/white colony screening of bacterial colonies. IPTG is also used in the induction of recombinant proteins. In those systems, a protein of interest is encoded downstream of the IPTG inducible promoter. In the presence of IPTG, the protein of interest is induced in the cell culture. The culture can then be lysed and the protein expressed and purified through a number of methods, including His Tag or GST purification systems (for proteins with ligand tags). GoldBio IPTG is made from a synthetic, non-animal origin. Functional Highlights and Mechanism IPTG acts by mimicking the natural inducer allolactose: it binds to the lac repressor (LacI) and causes its release from the lac operator site, allowing transcription of downstream genes under the lac promoter. Because IPTG is not metabolized by the cell, its concentration remains stable over time, enabling sustained induction rather than being depleted. In recombinant protein expression systems (for example vectors using T7 promoter under lac operon regulation), addition of IPTG triggers expression of the gene of interest downstream of the inducible promoter. IPTG is often used in colony screening (e.g., blue/white screening) in combination with chromogenic substrates such as X‑Gal: in this context IPTG activates β-galactosidase expression which cleaves X-Gal to yield a colored product. Because of the consistency and high quality of GoldBio’s IPTG, it supports reproducible gene induction workflows and reduces variability associated with induction reagent quality. Applications Gene expression induction in systems controlled by the lac operon Blue-white screening (with X-Gal) for recombinant DNA identification Controlled production of recombinant proteins Timed gene activation for functional studies Regulatory input in synthetic biology circuits Research Applications for IPTG (Click each for more information) Induction of Protein Expression in Lac Operon-Based Systems Purpose: To induce recombinant protein expression in bacterial systems, particularly Escherichia coli. How It Works: IPTG is a non-metabolizable analog of allolactose that binds to the LacI repressor, causing dissociation from the lac operator and activation of transcription from lac-derived promoters. Applications: High-yield recombinant protein production using pET, pGEX, pMAL, and related expression systems. Studier, F. W., & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. Journal of Molecular Biology, 189(1), 113–130. Blue/White Screening in Cloning Purpose: To differentiate recombinant clones from non-recombinant colonies during cloning workflows. How It Works: IPTG induces β-galactosidase expression; in the presence of X-gal, colonies with intact lacZα appear blue, while recombinant colonies with disrupted lacZ remain white. Applications: Screening workflows using pUC19, pBluescript, and other multiple cloning site-containing vectors. Vieira, J., & Messing, J. (1982). The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene, 19(3), 259–268. Study of Gene Regulation and Promoter Function Purpose: To investigate transcriptional regulation and promoter-controlled gene expression. How It Works: IPTG induces reporter genes such as GFP or luciferase downstream of lac-based promoters, enabling quantitati
• Notacow™ rAlbumin (Recombinant Human Serum Albumin) — Notacow™ rAlbumin is a premium recombinant human serum albumin (rHSA) produced using a proprietary fungal expression platform and manufactured entirely without animal-derived materials. Designed as a high-performance alternative to plasma-derived albumin, Notacow™ rAlbumin delivers the functionality of native human serum albumin while providing exceptional purity, lot-to-lot consistency, and supply reliability. Unlike plasma-derived albumin, Notacow™ rAlbumin is animal-origin-free, hormone-free, and immunoglobulin-free, eliminating many of the variability and contamination concerns associated with biological source materials. Its recombinant production process provides a highly reproducible protein ideally suited for sensitive research, diagnostic, and bioprocessing applications. Whether used as a carrier protein, stabilizer, media supplement, or formulation component, Notacow™ rAlbumin offers dependable performance without relying on human plasma or animal-derived ingredients. Why Choose Notacow™? Researchers increasingly require reagents that deliver reproducible results while supporting animal-free workflows. Notacow™ rAlbumin combines the proven functionality of human serum albumin with the advantages of recombinant fungal expression to provide a highly consistent protein free from plasma-derived variability, hormones, and immunoglobulins. The result is a dependable albumin source for advanced cell culture and next-generation biologics. Notacow™ Advantages Animal-Origin-Free Hormone-Free Immunoglobulin-Free Recombinant Fungal Expression High Purity (≥98%) Exceptional Lot-to-Lot Consistency Key Features & Benefits Animal-Origin-Free – Produced without animal-derived materials or plasma components. Hormone-Free – Manufactured without endogenous animal or human hormones that may interfere with sensitive biological assays. Immunoglobulin-Free – Free of immunoglobulins commonly present in serum-derived albumin, reducing background interference and improving assay reproducibility. Recombinant Human Serum Albumin – Structurally and functionally comparable to native human serum albumin. Fungal Expression System – Produced using recombinant fungal cells for scalable, reliable manufacturing. High Purity – Purified to minimize host-cell proteins and process-related impurities. Exceptional Lot-to-Lot Consistency – Recombinant production ensures reproducible performance across manufacturing batches. Enhanced Safety Profile – Eliminates risks associated with plasma-derived contaminants and adventitious agents. Reliable Global Supply – Fermentation-based production removes dependence on plasma collection and animal-derived raw materials. Technical Specifications Property Specification Product Type Recombinant Human Serum Albumin (rHSA) Expression System Fungal cells Animal-Origin Status Animal-Origin-Free Hormones Not Detected / Hormone-Free Immunoglobulins Not Detected / Immunoglobulin-Free Form Lyophilized powder Purity ≥98% Total Protein (Dry Basis) ≥90% Moisture ≤5% Molecular Weight ~66.5 kDa pH (10% Solution) 6.5–7.5 Storage 2–8°C Applications Notacow™ rAlbumin is ideal for applications where consistency, purity, and animal-free manufacturing are essential, including: Mammalian and stem cell culture Serum-free and chemically defined media Cell and gene therapy research Diagnostic assay development Immunoassays and molecular diagnostics Biopharmaceutical formulation Vaccine development and manufacturing Protein and enzyme stabilization Drug delivery research Cryopreservation media Bioprocess development Storage/Handling Dry powder should be stored at 2-8°C, protected from the light.

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Public source evidence

• GoldBio
• Contact – GoldBio
• Dr. Gold's Bacterial Protein Extraction Reagent – GoldBio
• Contact Your Gold Biotechnology® Rep – GoldBio
• Notacow™ rAlbumin (Recombinant Human Serum Albumin) – GoldBio
• Citation Search Tool – GoldBio
• Newly Listed Products – GoldBio
• IPTG | High-Purity Inducer | CAS# 367-93-1 – GoldBio