Immune Response

CD Antibodies are commonly used as cell markers, with cells being defined based on what molecules are present on their surfaces. CD molecules can act in numerous ways including acting as receptors or ligands. CD proteins can have other functions such as cell adhesion. 

Mitogen-activated protein kinases (MAPKs) are a family of highly conserved protein kinases involved in a variety of cellular processes. MAPKs include extracellular signal-regulated kinase 1 and 2 (ERK1/2), and c-Jun N terminal kinase 1-3/stress activated protein kinases (SAPKs)

Heat shock proteins (HSPs) are present in most cells, serving as molecular chaperones, and they play a role in cell protection from damage in response to stress stimuli. These capabilities make HSPs excellent for studying pathogenesis of diseases. These include autoimmmunity (inflammatory response), neurodegenerative disease, certain cancers and atherosclerosis.

Heat-shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 refer to families of heat shock proteins on the order of 60, 70 and 90 kilodaltons in size, respectively

These belong to the broad category of cytokines and chemokines. The related proteins play a role in growth, differentiation, and activation functions that regulate and determine the nature of immune responses and control immune cell trafficking and the cellular arrangement of immune organs. Which cytokines are produced in response to an immune insult determines initially whether an immune response develops and subsequently whether that response is cytotoxic, humoral, cell-mediated, or allergic.

Matrix Metalloproteinases (MMPs) are a family of zinc metalloendopeptidases secreted by cells, and are responsible for much of the turnover of matrix components. They are produced as zymogens, with a signal sequence and propeptide segment that must be removed during activation. In general, This signal sequence and propeptide plus a catalytic domain (containing the highly conserved zinc binding site) characterizes the structure of the MMPs.

MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

More antibodies for the immune response research. 

Antibodies for studying neuropathic, nociceptive and inflammatory pain.

Transforming growth factor (sometimes referred to as Tumor growth factor, or TGF) is used to describe two classes of polypeptide growth factors, TGFα and TGFβ.

• TGFα is upregulated in some human cancers. It is produced in macrophages, brain cells, and keratinocytes, and induces epithelial development.
• TGFβ exists in three known subtypes in humans, TGFβ1, TGFβ2, and TGFβ3. These are upregulated in some human cancers, and play crucial roles in tissue regeneration, cell differentiation, embryonic development, and regulation of the immune system. Isoforms of transforming growth factor-beta (TGF-β1) are also thought to be involved in the pathogenesis of pre-eclampsia. TGFβ receptors are single pass serine/threonine kinase receptors.

Toll like receptors (TLR) are highly conserved throughout evolution and have been implicated in the innate defense to many pathogens. In mammals, TLR identified as type I transmembrane signaling receptors with pattern recognition capabilities have been implicated in the innate host defense to pathogens.

These microbial molecular markers may be composed of proteins, carbohydrates, lipids, nucleic acids and/or combinations thereof. Individual TLRs recognize distinct pathogen-associated PAMPs, initiating signaling cascades that promote the immune response. Structurally, TLRs are type I transmembrane receptors that possess varying numbers of extracellular N-terminal leucine-rich repeat (LRR) motifs, followed by a cysteine-rich region, a TM domain, and an intracellular Toll/IL-1 R (TIR) motif.

Wnt proteins are key regulators of embryonic development. Many receptors and inhibitors influence the Wnt-signaling pathway to ultimately regulate beta-Catenin stability and availability. Understanding Wnt and beta-Catenin signaling and the role of their antagonists (including Frizzled proteins) is important to elucidating the events controlling stem cell organization and maintenance, embryonic development, tissue differentiation, cell adhesion and migration, as well as tumorigenesis and cancer induction and progression.