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Dual specificity mitogen-activated protein kinase kinase 3 (MAP2K3) is a dual specificity protein kinase which is a member of the MAP kinase kinase family. MAP2K3 is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. MAP2K3 phosphorylates and consequently activates MAPK14/p38-MAPK.

MAPK11 belongs to the MAP kinase family and is most associated with p38 MAP kinases (MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. MAPK11 cooperates with HDAC3 and Promyelocytic leukemia protein and takes part in a signal transduction pathway which is activated by alterations in the osmolarity of the extracellular environment, by environmental stress, or by cytokines.

JUN N-terminal Kinase 2is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

E.Coli Acetate Kinase, also knowns as ACKA, catalyzes the formation of acetyl phosphate from acetate and ATP and also catalyzes the reverse reaction. ACKA takes part in synthesis of various ATP formed catabolically during anaerobic growth of the organism.

Serine/threonine-protein kinase 3 (), is a mammalian Ste20-related protein kinases most closely related to Drosophila Hippo, which is a major regulator of cell proliferation as well as survival in the course of development. STK3 is a serine/threonine kinase which functions early in a pheromone responsive signal transduction cascade in yeast. Furthermore, STK3 activates the human large tumor suppressor kinase Lats1. STK3 also modulates stress-induced cardiac hypertrophy.

Extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinaseintracellular signalingmolecules which are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virusinfection, ligands for heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway.
The term, "extracellular signal-regulated kinases", is sometimes used as a synonym for mitogen-activated protein kinase(MAPK), but has more recently been adopted for a specific subset of the mammalianMAPK family. In the MAPK/ERK pathway, Rasactivates c-Raf, followed by MEKand then MAPK1/2 (below). Ras is typically activated by growth hormones through receptor tyrosine kinasesand GRB2/SOS, but may also receive other signals. ERKs are known to activate many transcription factors and some downstream protein kinases. Disruption of the ERK pathway is common in cancers, especially Ras, c-Raf and receptors such as HER2.Mitogen-activated protein kinase 3 (MAPK3) is also known as "extracellular signal-regulated kinase 1" (ERK1). Transgenic gene knockoutmice lacking MAPK3 are viable and it is thought that MAPK1 can fulfill most MAPK3 functions in most cells. The main exception is in T cells. Mice lacking MAPK3 have reduced T cell development past the CD4+CD8+ stage.

The protein kinase A holoenzyme is a heterotetramer composed of two types of subunits: Catalytic and Regulatory. The Catalyticsubunit contains the enzyme's active site. It also contains a domain that binds ATP and a domain that binds the regulatory subunit. The Regulatory subunit consists oftwo molecules which bind one another in an anti-parallel orientation to form a homodimer; for type I subunits- this binding is covalent via disulfide bonds. This subunit also has has two domains that bind cyclic AMP, a domain that interacts with a catalytic subunit, and an "auto-inhibitory" domain that serves as a substrate or pseudosubstrate for the catalytic subunit. Regulatory subunits may also have biologic activity distinct from their role in modulating catalytic subunit activity. Regulatory subunits exist in two major forms, RI and RII, with each form having two subtypes designated alpha and beta. Each of the four isotypes of the regulatory subunit is encoded by a different gene. In addition, three isotypes of the catalytic subunit have been identified (alpha, beta and gamma). The different isotypes tend to have different distributions within cells and among tissues. Type I enzymes inhabit cytoplasmic, soluble fractions of the cell, whereas type II enzymes tend to associate with cellular membranes.

Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinasessuch as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity. The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that RasGTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK). Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation. Transgenic gene knockoutmice lacking MAPK1 have major defects in early development.

Protein Phosphatase 1F (PPM1F) is a part of the PP2C family of Ser/Thr protein phosphatases whose members are known to be negative regulators of cell stress response pathways. PPM1F interacts with Rho guanine nucleotide exchange factors (PIX), and as a result blocks the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is one of the substrates of PPM1F. PPM1F is found to be an apoptosis Promoter.

Mitogen-Activated Protein Kinase 6 (MAP2K6) is a part of the dual specificity protein kinase family. MAP2K6 phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. MAP2K6 is a vital component of the MAP kinase signal transduction pathway. MAP2K6 takes part in various cellular processes such as stress induced cell cycle arrest and apoptosis.

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle''s disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

cAMP-dependent protein kinase inhibitor beta (PKIB) belongs to the cAMP-dependent protein kinase inhibitor family. PKIB may interact with the catalytic subunit of cAMP-dependent protein kinase and function as a competitive inhibitor.

Thymidine kinase 2 mitochondrial (TK2) is a member of the DCK/DGK family. TK2 is an enzyme, a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. Thymidine kinase is found in most living cells. Thymidine kinase is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases have a central function in the synthesis of DNA and thus in cell division, since they are part of the exceptional reaction chain to introduce deoxythymidine into the DNA. TK2 is a deoxyribonucleoside kinase which specifically phosphorylates thymidine, deoxycytidine, and deoxyuridine. TK2 localizes to the mitochondria and is essential for mitochondrial DNA synthesis. TK2 gene defects are a cause of mitochondrial DNA depletion syndrome type 2 (MTDPS2).

PIM1, which is a part of the Ser/Thr protein kinase family and PIM subfamily, is expressed primarily in B-lymphoid and myeloid cell lines, and is overexpressed in hematopoietic malignancies and in prostate cancer. PIM1 functions as Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation, consequently providing a selective advantage in tumorigenesis. Both human and orthologous mouse genes have been reported to encode two isoforms resulting from the use of alternative in-frame translation initiation codons, the upstream non-AUG (CUG) and downstream AUG codons.

Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.

The Casein kinase 2 (EC 2.7.11.1) is a serine/threonine-selective protein kinase that is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes. Casein kinase 2 activity has been reported to be activated following Wnt signaling pathway activation. A Pertussis toxin-sensitive G protein and Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2. Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.

The MAP2K1 protein is encoded by the MAP2K1 gene. This enzyme serves as a MAP (mitogen activated protein) kinase, it is a part of the dual specificity protein kinase family. Extracellular signal-regulated kinases such as MAP kinases has an important role in assimilation of various biochemical signals. MAP2K1 is located upstream to the MAP kinases and activates them by multiple intra and extracellular signals. The enzyme serves as a key factor in the signal transduction pathway of MAP kinase, therefore it takes part in the cell development (transcription regulation, proliferation, differentiation etc.).

ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.

MAPK12 is a member of the MAP kinase family. MAPK12 acts as a signal transducer during differentiation of myoblasts to myotubes. p38 proteins utilizes magnesium as a cofactor to catalyze the ATP-dependent phosphorylation of target proteins and is produced in several regions all over the body with common expression patterns in heart.

CIB2 is a member of the calcium and integrin-binding family.CIB2 is possibly a Ca2+-binding regulatory protein which interacts with DNA-dependent protein kinase catalytic subunit (DNA-PKcs). In the skeletal muscle, CIB2 co-localizes with the integrin alpha7B subunit at the sarcolemma and at the neuromuscular and myotendinous junctions. CIB2 is closely related to CIB1.

Serine/threonine kinase 17b (STK17B) is a member of the protein kinase superfamily. STK17B functions as a positive regulator of apoptosis. STK17B interacts with CHP1; this interaction stimulates CHP1 to translocate from the Golgi to the nucleus. STK17B is highly expressed in the placenta, lung, pancreas, however it has lower levels in the heart, brain, liver, skeletal muscle and kidney.

Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.

Extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinaseintracellular signalingmolecules which are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virusinfection, ligands for heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway. The term, "extracellular signal-regulated kinases", is sometimes used as a synonym for mitogen-activated protein kinase(MAPK), but has more recently been adopted for a specific subset of the mammalianMAPK family. In the MAPK/ERK pathway, Rasactivates c-Raf, followed by MEKand then MAPK1/2 (below). Ras is typically activated by growth hormones through receptor tyrosine kinasesand GRB2/SOS, but may also receive other signals. ERKs are known to activate many transcription factors and some downstream protein kinases. Disruption of th