Proteins & Peptides

LL-37 is a cleaved antimicrobial residue peptide of hCAP18 (human cationic antimicrobial protein, 18kDa) in the family of cathelicidin. Cathelicidins are predominantly found in the peroxidase negative granules of neutrophils. And it has been shows broad antimicrobial activity towards gram negative and gram positive bacteria.

Translocation through the plasma membrane has been shown to be a major limiting step for the delivery of various macromolecules to the cytoplasm and other intracellular compartments (e.g., mitochondria, nucleus). Numerous studies have confirmed that specific peptide sequences known as cell penetrating peptides (CPP) derived from proteins able to cross the plasma membrane, can be added to various cargo and delivered across cell membranes. The cargo molecules that have been successfully transported into cells includes oligonucleotides, peptides, peptide nucleic acids, proteins and nanoparticles. One of these translocating peptides was derived from the HIV-1 Tat protein, specifically located within the first exon of the HIV tat protein. The specific HIV tat sequence is highly basic (cationic) and is readily added to peptides either as a preformed peptide with a site for direct conjugation to other molecules (typically a cysteine). Addition of the tat-cargo complex (5-50 uM concentrat

β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Lactase is often confused as an alternative name for β-galactosidase, but it is actually simply a sub-class of β-galactosidase. β-galactosidase is an exoglycosidase which hydrolyzes the β-glycosidic bond formed between a galactose and its organic moiety. It may also cleave fucosides and arabinosides but with much lower efficiency. It is an essential enzyme in the human body, deficiencies in the protein can result in galactosialidosis or Morquio B syndrome. In E. coli, the gene of β-galactosidase, the lacZ gene, is present as part of the inducible system lac operon which is activated in the presence of lactose when glucose level is low. It is commonly used in molecular biology as a reporter marker to monitor gene expression. It al

GST (Glutathione-S-Transferase) is a 26kDa protein. GST is a fusion protein in an array of prokaryotic expression vectors, including the pGEX family of vectors. Anti-GST antibodies GST will detect the expressed GST protein or a GST-fusion protein, and can be utilized for immuno-purification of GST-fusion proteins.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both heavy and light chains of the antibody molecule are present.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. This product possesses the F(ab) region possessing the epitope-recognition site, both heavy and light chains of the antibody molecule are present.

Bovine Collagen Type I is one of a family of proteins found particularly in the flesh and connective tissues of mammals (approximately one-third of the body's total protein). Over two dozen types of collagen have been described; Type I is the most abundant form in the body. Collagen Type I is found in scar tissue, tendons, the skin, arterial walls, the corneas, muscles, cartilage, and in the organic parts of bones and teeth. Bovine Collagen Type I is ideal for investigators involved in extracellular matrix proteins and osteoporosis.

Bovine Collagen Type II (Nasal Cartilage) is one of a family of proteins found particularly in the flesh and connective tissues of mammals (approximately one-third of the body's total protein). Over two dozen types of collagen have been described; Type II is found predominantly in hyaline cartilage (50% of the protein in hyaline is collagen type II) and is also found in the vitreous humor of the eye.