A situation when a fitness enthusiast knows what to do but hasn’t done it yet. An abyss may hinder his progress at the gym. For example, a bloke knows leg day exercises but is having second thoughts.

In order for the squat to be considered “Ass to Grass” the athlete has to squat below the parallel level. You don’t have to necessarily touch your ankles with your glutes to achieve this.

Your hip crease has to be parallel with your knee cap. If you are planning on competing I would recommend squatting slightly below the parallel level just so that the judges would not have any room for doubt.

Some machines feature complicated pulley systems and do not reflect the actual weight you are lifting.
1:1 Ratio – this means that the machine has no mechanical advantage and that you are lifting the weight which you have loaded on the carriage/weight stack.
2:1 Ratio – this means this machine’s pulley system provides a mechanical advantage and you are lifting half of the loaded weight.
3:1 Ratio – you are lifting a third of the loaded weight.

These are the specific items that you will receive when you purchase the product. Some products are shown with items that are not included for demonstration purposes.

The height of the highest position of the bench.

The overall thickness of the pad including the base board and the padding.

Back Rest Pads vary in shape and size depending on the intended purpose of the bench.
Bodybuilding – If you are into bodybuilding or have shoulder problems, we recommend opting for a bench with a narrower backrest pad at the top. It allows your shoulders to sit outside of the bench giving them more room to move around.
Powerlifting – The standard height and with of IPF specification bench is 45 cm x 30 cm. This gives you the best possible stability for your heavy lifts.
General Strength Training – Unless you are training for any of the specific goals above, all our benches are suitable for general strength work. They are all robust and durable.

Raw steel will rust without some form of coating. There are various coatings – paint, powder coat, chrome, zinc oxide, zinc plating, titanium plating, etc. All these coatings can also contribute to the aesthetic appeal of the gym equipment.

Prevents you from sliding off the bench during exercises like incline press.

Decline Bench Press: -15° – Targets your lower pectoral muscles.

Flat Bench Press: 0° – Targets your pectoral muscles.
Incline Bench Press: 35°- 45° – Targets your upper chest.
Shoulder Press: 60°-90° – Targets your shoulders.

The height of the bench in a flat position. IPF (International Powerlifting Federation) standard is 45 cm.

The thickness of the Steel/Tubing – this measurement refers to the width and depth of the square tube/upright used in the construction.
The thickness of the Uprights – this measurement refers to the thickness of the steel involved in the construction.
Rubber Feet – protects your floor from scratches and improves stability.

Domestic – Designed to be used in a home, garage gym or a small studio.
Studio – Designed for use in a studio/small commercial gym and is certified for studio use by European Standards EN 20957 I.II.IV Class H.
Commercial – Designed for use in a commercial setting and is certified for commercial use by European Standards EN 20957 I.II.IV Class S.

The base weight of the item, without any packaging.

Casein is a family of related phosphoproteins (αS1, αS2, β, κ). These proteins are commonly found in mammalian milk, comprising c. 80% of the proteins in cow’s milk and between 20% and 45% of the proteins in human milk. Sheep and buffalo milk have a higher casein content than other types of milk with human milk having a particularly low casein content.

Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. The most common form of casein is sodium caseinate. In milk, casein undergoes phase separation to form colloidal casein micelles, a type of secreted biomolecular condensate.

As a food source, casein supplies amino acids, carbohydrates, and two essential elements, calcium and phosphorus.

Casein contains a high number of proline residues, which do not interact. There are also no disulfide bridges. As a result, it has relatively little tertiary structure. It is relatively hydrophobic, making it poorly soluble in water. It is found in milk as a suspension of particles, called casein micelles, which show only limited resemblance with surfactant-type micelles in a sense that the hydrophilic parts reside at the surface and they are spherical. However, in sharp contrast to surfactant micelles, the interior of a casein micelle is highly hydrated. The caseins in the micelles are held together by calcium ions and hydrophobic interactions. Any of several molecular models could account for the special conformation of casein in the micelles. One of them proposes the micellar nucleus is formed by several submicelles, the periphery consisting of microvellosities of κ-casein. Another model suggests the nucleus is formed by casein-interlinked fibrils. Finally, the most recent model proposes a double link among the caseins for gelling to take place. All three models consider micelles as colloidal particles formed by casein aggregates wrapped up in soluble κ-casein molecules.

The isoelectric point of casein is 4.6. Since milk’s pH is 6.6, casein has a negative charge in milk. The purified protein is water-insoluble. While it is also insoluble in neutral salt solutions, it is readily dispersible in dilute alkalis and in salt solutions such as aqueous sodium oxalate and sodium acetate.

The enzyme trypsin can hydrolyze a phosphate-containing peptone. It is used to form a type of organic adhesive.

Hydrolysate refers to any product of hydrolysis. Protein hydrolysate has special application in sports medicine because its consumption allows amino acids to be absorbed by the body more rapidly than intact proteins, thus maximizing nutrient delivery to muscle tissues. It is also used in the biotechnology industry as a supplement to cell cultures. In the December 2013 edition of The International Journal of Food Science and Technology, hydrolysate was shown to be rich in L-aspartic acid and the necessary minerals manganese and selenium

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells, and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; but in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by post-translational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Some proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.

Once formed, proteins only exist for a certain period and are then degraded and recycled by the cell’s machinery through the process of protein turnover. A protein’s lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.

Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyse biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. In animals, proteins are needed in the diet to provide the essential amino acids that cannot be synthesized. Digestion breaks the proteins down for use in the metabolism.

Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.

These are portable parallel bars which help increase upper body and core strength.