Proteins & Peptides

The p39 protein, or Basic membrane protein A, is one of the immunogenic cell membrane components of Borrelia burgdorferi, the spirochete carried by Ixodes ticks. The spirochete migrates from the tick midgut during feeding to its salivary glands and are thus transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes. It is believed that expression of the various proteins associated with the spirochete may be regulated by the changes in tick life cycle, changes in conditions during tick feeding (such as temperature, pH, and nutrients) and/or in coordination with the course of infection of the mammal host. BmpA is expressed during the invasion of the spirochete and in the evolution of the arthritis of Lyme disease in mammals. It belongs to the BMP lipoprotein family. The major products of the B. burgdorferi basic membrane protein (bmp) A/B operon that are induced in murine and human joints possess inflammatory properties.

CRASP-1, or Complement Regulator-Acquiring Surface Protein 1, is a multifunctional protein of Lyme disease-causing B. burgdorferi that binds to several human extracellular matrix proteins and plasminogen, including factor H (resulting in inhibition of complement activation in mammals) and Human Bone Morphogenic Protein 2. These interactions may contribute to adhesion, bacterial colonization, and organ tropism and may allow dissemination of B. burgdorferi in the host. B. burgdorferi spirochetes express up to 5 complement regulator-acquiring surface proteins. Multiple copies of sequences analagous to CRASP-1 genes have been detected in Borrelia plasmids. Borrelia species contain a large number of plasmids, of linear and circular, some of which appear to repeat sequences or contain fragments of other genes. These regions may serve as potentially usable information for the survival of Borrelia in its multiple environments during its life cycle. In addition, the sequence for CRASP-1

CRASP-2 (Complement Regulator-Acquiring Surface Protein 2) of Borrelia burgdorferi binds FHL-1 and factor H binding protein in a distinct way. It may be predominantly expressed by serum-resistant Borrelia strains. Borrelia burgdorferi sensu lato has the ability to evade immune systems to persist in a variety of vertebrate hosts. This activity is dependent on a number of factors. Some Borrelia species bind host-derived fluid-phase immune regulators FHL-1 and factor H to their surface via complement regulator-acquiring surface proteins (CRASPs). Factor H and FHL-1 serve as cofactors for factor I, a serine protease that cleaves complement component 3b (C3b) directly on the cell surface and thereby confers resistance of spirochetes to complement-mediated lysis. It is possible that because of discontinuous binding regions in the factor H/FHL-1, long distance interaction may be involved in binding of both immune regulators. Putative coiled-coil structural elements may be important in

Surface Lipoprotein p27 of Borrelia burgdorferi is a surface-exposed lipoprotein that has been shown (by Western blot and Northern blot) to be expressed in the European B. burgdorferi strain B29, but not in the American strain B31. Cell envelope proteins of bacterial pathogens play important roles in the host-parasite interactions that occur during infection, including cell adherence, cell invasion, and immune cell activation or evasion. p27 is a basic protein of 248 amino acids with a typical prokaryotic leader sequence of 17 amino acid residues at the N-terminus of the proposed translation product. The p27 gene is located on a linear plasmid of a size of approximately 55 kb. Borrelia spirochetes are unique among diderm bacteria in their abundance of surface-displayed lipoproteins, some of which play important roles in the pathogenesis of Lyme disease and relapsing fever. There is evidence that Borrelia lipoproteins are specifically targeted to the bacterial surface, but that the

Variable Lipoprotein Surface-Exposed protein, or VlsE, is a lipoprotein on the surface of the Lyme Disease spirochete Borrelia burgdorferi, detectable during all its life stages. It can exist as many different isoforms. VlsE has variable regions (VRs) and invariable regions (IRs). Some IRs are anchored in the outer membrane of the bacteria and some are antigens exposed on the membrane surface. Replacement of the VR by Borrelia within days of being transferred to a mammalian host presents new surface antigens to the host immune system, and helps Borrelia avoid a strong reaction by host immune systems. The VlsE is apparently not modified as much in the tick or in the rodent vector, when compared to in the mammal host. Several putative envelope proteins of B. burgdorferi appear to be expressed only in the infected mammalian host. The VRs are antigenic, irregularly shaped loops on the bacterial surface which may help to hide both membrane-incorporated and surface portions of adjacen

AKT2 Control peptide is for use in control assays with Anti-AKT2 (p/n 200-501-E71). AKT2 Antibody detects AKT2 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation.

Mitogen-activated protein kinase kinase 1, also known as MKK or MEK, is an integral component of the MAP kinase cascade that regulates cell growth and differentiation. This pathway also plays a key role in synaptic plasticity in the brain. Activated MEK 1 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. MEK1 and MEK2 are about 80% identical to each other, and nearly identical within the kinase domain. MEK1 is ideal for investigators involved in Neuroscience, Cell Signaling and Cancer Research.

Mitogen-activated protein kinase kinase 2, also known as MEK2 or MKK2, is an integral component of the MAP kinase cascade that regulates cell growth and differentiation. This pathway also plays a key role in synaptic plasticity in the brain. Activated MEK 2 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. MEK1 and MEK2 are about 80% identical to each other, and nearly identical within the kinase domain. MEK2 is ideal for investigators involved in Neuroscience, Cell Signaling and Cancer Research.

Mitogen activated protein kinase 3, also known as MAPK3, ERK, or ERK1, is an integral component of the MAP kinase cascade that regulates cell growth and differentiation. ERK1 and ERK2 are activated by MEK1 and MEK2 in the B-raf signaling pathway resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Human ERK1 and ERK2 are 84% identical in sequence and share common functionality in cells. ERK1 is ideal for investigators involved in Neuroscience, Cell Signaling and Cancer Research.