Standard used for determining protein concentration by CB protein assay. This coomassie dye-based protein assay provides simple, rapid estimation of protein concentration and can be performed using as little as 1mg protein per sample. CB-Protein Assay is supplied ready to use with an easy…

Protein with numerous biochemical applications including ELISAs, immunoblots, and immunohistochemistry Biotechnology Grade Heat shock isolation Appearance: white to off-white powder pH (5% water): 6.5-7.5 Heavy Metals (Pb): DNase: None detected RNase: None detected Protease: None…

Reagent grade, fatty acid free Moisture: < 1.0% Heavy metals: <0.5% Endotoxin: ≤0.1EU/mg pH (10% water): 6.5 - 7.5

Acetylated to inactivate nucleases commonly found in BSA. Acetylated BSA should not be used as a protein standard since acetylation of tyrosine residues prevents color development in the Lowry assay and other similar protein determinations. It is prepared by a modified method of the Cohn cold…

Functions by binding to hemoglobin. 98.0% (HPCE), powder, color off-white Occurs as 3 major phenotypes: type 1-1, type 2-1, type 2-2

bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product, food additive or as a household chemical.

A biotin-binding glycoprotein prepared from chicken egg white, Molecular weight=67kDa, pI = 10 Glycosylation and isoelectric point make avidin more soluble than streptavidin Significantly less expensive than recombinant streptavidin protein Based on strong binding with biotin, avidin is…

CAS 9048-46-8 Cold Alcohol Isolation Biotechnology grade Purity (Electrophoresis): >99% Moisture DNase/RNase: None Detected Ash: 0.5% Heavy Metals: 0.005% Storage: 2-8°C

Conalbumin (ovotransferrin), Gal d3, is the second most common protein in egg-white. It is a plasma protein that is responsible for binding and transporting iron. Conalbumin is a major allergen of hen's egg-white.

1mg/ml BSA solution in 0.85% Sodium Chloride and 0.01% Sodium azide.