Category: Proteins & Peptides

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  • Brand: Abclonal
  • Brand: Axol
  • Brand: Biosensis
  • Brand: Boster
Reference: PE-1749-50

Synthetic beta-amyloid Aβ1-42 was monomerized by HFIP (hexafluoro-2-propanol) treatment and dried. One vial contains 50 μg monomeric Aβ peptide that can be used to form solutions of unaggregated Aβ monomers, aggregated Aβ oligomers, Aβ fibrils and Aβ protein complexes according to published protocols, and used in a variety of research applications.

Reference: PE-1750-1000

A proprietary preparation of human amyloid beta peptide (amino acids 1-42) that was initially monomerized by HFIP-treatment and then allowed to form oligomers by the procedure described in Youmans KL et al., 2012, followed by lyophilisation using Biosensis' proprietary stabilization procedures.

The resulting oligomeric mixture has been specially designed to allow the formation of stable, oligomeric Aβ1-42 peptide, multimeric complexes or oligomers. The material is intended to be used as a stable and consistent standard or positive control for oligomeric ELISA assays, as well as other research applications.

Reference: RP00001

Tumor necrosis factor alpha (TNF-alpha), also known as TNF, TNFA or TNFSF2, is the prototypic cytokine of the TNF superfamily. This cytokine is mainly secreted by macrophages. It can bind to, and thus functions through its receptors TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. This cytokine is involved in the regulation of a wide spectrum of biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. This cytokine has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer. KNockout studies in mice also suggested the neuroprotective function of this cytokine.

Reference: RP00002

Interleukin-1 beta (IL1 beta or IL1B) also known as catabolin, is a member of the interleukin 1 cytokine family.This cytokine is produced by activated macrophages as a proprotein, which is proteolytically processed to its active form by caspase 1 (CASP1/ICE). This cytokine is an important mediator of the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. The induction of cyclooxygenase-2 (PTGS2/COX2) by this cytokine in the central nervous system (CNS) is found to contribute to inflammatory pain hypersensitivity.

Reference: RP00003

Interleukin-1 receptor antagonist (IL-1RA) also known as IL1RN is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. A polymorphism of this protein is reported to be associated with increased risk of osteoporotic fractures and gastric cancer.

Reference: RP00004

Interleukin-6 (IL-6) is a multifunctional α-helical cytokine that regulates cell growth and differentiation of various tissues, which is known particularly for its role in the immune response and acute phase reactions. The encoded protein has been shown to be an endogenous pyrogen capable of inducing fever in people with autoimmune diseases or infections. The protein is primarily produced at sites of acute and chronic inflammation, where it is secreted into the serum and induces a transcriptional inflammatory response through interleukin 6 receptor, alpha. The functioning of this protein is implicated in a wide variety of inflammation-associated disease states, including suspectibility to diabetes mellitus and systemic juvenile rheumatoid arthritis.

Reference: RP00005

The protein is localized in the endoplasmic reticulum (ER) and golgi, and is also secreted. Reducing expression of this protein increases susceptibility to ER stress-induced death and results in cell proliferation. Activity of this protein is important in promoting the survival of dopaminergic neurons. The presence of polymorphisms in the N-terminal arginine-rich region, including a specific mutation that changes an ATG start codon to AGG, have been reported in a variety of solid tumors; however, these polymorphisms were later shown to exist in Normal tissues and are thus no longer thought to be tumor-related.

Reference: RP00007

Galectin-1, also known as LGALS1 (lectin, galactoside-binding, soluble 1), is a 135 amino acid (aa), 14 kDa, pleiotropic, Non-glycosylated, monomeric or homodimeric carbohydrate-binding protein of the prototype galectin family. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments, or secreted by non-classical pathways. Secreted Galectin-1 has immunosuppressive and anti-inflammatory properties and suppresses acute and chronic inflammation and autoimmunity. It contributes to negative selection of developing T cells, immunosuppression by regulatory T cells, resolution of the inflammatory response, and inhibition of immune cell migration, inflammatory cytokine production, and mast cell degranulation. Galectin-1 contributes to different steps of tumour progression including cell adhesion, migration and tumour-immune escape, suggesting that blockade of galectin-1 might result in therapeutic benefits in cancer. Several potential glycoprotein ligands for galectin-1 have been identified, including lysosome-associated membrane glycoproteins and fibronectin, laminin, as well as T-cell glycoproteins CD43 and CD45. Evidence points to Gal-1 and its ligands as one of the master regulators of such immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host-pathogen interactions.