Specials
10% Discount on select Affinity Purification Packages for a limited time only!!

In the News

Humanin: Neuroprotection Against Neurodegenerative Diseases

Neuronal cell death is a pathological hallmark of Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS) and prion protein diseases (PrP). Therapy directed at eliminating the primary neurotoxic event that leads to cell death may be very effective against neurodegenerative diseases.

Several studies in the literature have now shown that an endogenously produced peptide, Humanin, can abolish cell death in neuronal cells.Humanin is a 24 amino acid secreted peptide encoded by both nuclear and mitochondrial genomes. (PNAS, 98:6336-6341, 2001, J Neurosci, 21:9235-9245, 2001, Neuroscience Letters, 324:227-231, 2002). Humanin has been shown to rescue cortical neurons from PrP118-135 fragment induced apoptosis (Mol Cell Neurosci, 25:95-102, 2004). Humanin also protected neurons from the neurotoxic effects of beta amyloid 1-42 and beta amyloid 25-35 (J Neurosci, 21:9235-9245, 2001).

Additional studies on various derivatives of Humanin reveal that replacing serine at position 14 with a glycine residue produced a peptide that was 500 to 1000 fold more potent than Humanin. Humanin S14G prevented the beta amyloid 25-35 induced impairment of short term memory in mice (Mol Cell Neurosci, 25:95-102, 2004, J Neurosci Res, 79: 714-723, 2004). Combining a 17 amino acid derivative of Humanin with the activity-dependent neurotrophic factor (ADNF) resulted in a derivative of Humanin, named Colivelin,that was 1000 fold more potent. Both Humanin and Colivelin are effective against mouse dementia and neuronal death induced by injection of beta amyloid. Colivelin also has been shown to be as effective as VEGF and IGF-1 in prolonging survival of ALS mice. Colivelin improves both motor performance and survival of ALS mice (J Neurosci, 25:10252-10261, 2005, BBRC, 343:793-798, 2006, CNS Drug Reviews, 12:113-122, 2006, Mol Neurobiol, 35:55-84, 2007).(more ...)

Bioactive Peptides Derived from Milk Proteins

Numerous bioactive peptides are encrypted within the primary structure of milk proteins and released during gastrointestinal digestion and the processing of food (J Dairy Sci, 76: 301-310, 1993, J Dairy Sci, 88: 2348-2360, 2005). Upon release, these peptides have been shown to display antithrombotic, antihypertension, immunomodulation, antimicrobial and mineral absorption activities as well as opioid agonist and antagonist behaviors.

The majority of milk content is comprised of casein and whey proteins. Caseins are phosphoproteins that consist of four major groups: alpha s1, alpha s2, beta and kappa. The main whey proteins are lactalbumin and lactoglobulin.

Bioactive peptides from kappa casein (169 amino acids) are derived from the hydrolyzed C-terminal fragment known as caseinomacropeptide (106-169). The phosphorylated form of caseinomacropeptide, kappacin, has been identified as a potent antimicrobial (Antimicrobial Agents Chemotherapy, 45:2309-2315, 2001, Antimicrobial Agents Chemotherapy, 49: 2322-2328, 2005). (more ...)

Antibodies Using MAP Technology

Generating antibodies to linear peptide sequences is straight forward. The linear peptide sequence is made, purified, solubilized in phosphate buffered saline (PBS, pH7.2) and then conjugated to a carrier protein (KLH, BSA, OVA). The conjugated material is injected into an animal and bleeds taken after the animal has been immunized and boosted several times. If the peptide has been successfully conjugated to the carrier protein an antibody to the injected peptide will almost always be generated. (more...)

Innate Immunity
Innate, or nonspecific, immunity refers to the basic resistance to disease that all plants and animals possess. The innate immune system is the first line of defense against microbial invasions. One component of the innate immune system is the host-defense antimicrobial peptides. These peptides are active against a broad range of pathogenic microorganisms including Gram-positive and Gram-negative bacteria, fungi, yeast and viruses. The antimicrobial peptides are a diverse group of peptides but are usually short (10-60 amino acids in length), amphipathic and can be either cationic or anionic. These antimicrobial peptides can be further classified according to their secondary structure: alpha helices, beta sheet, extended helices and loops. The toxicity of antimicrobial peptides to bacteria has not yet been fully elucidated but it is believed that these peptides act by disrupting the bacterial cell membrane. (more..)