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2-Chloro-4-phenylnicotinonitrile
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2-Chloro-4-phenylnicotinonitrile
Catalog Number:
(89146-564)
Supplier:
Enzo Life Sciences
Description:
Inhibitor of serine proteinases having a chymotrypsin-like specificity like α-, β-, δ- and γ-chymotrypsin, chymases, cathepsin G, and most cysteine proteinases including papain and cathepsin A, B, H, and L.
Catalog Number:
(75932-158)
Supplier:
Rockland Immunochemical
Description:
Serine palmitoyltransferase (SPT), which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl-CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. SPT2 is the long chain base subunit 2 of mammalian serine palmitoyltransferase. SPT2 is catalytically active but needs its related protein SPT1 for its stabilization and anchoring the holoenzyme to the cytosolic face of the endoplasmic reticulum. As in the case with SPT1, mutations in the SPT2 gene can cause hereditary sensory and autonomic neuropathy type I (HSAN-I), resulting from a loss of SPT activity as well as the accumulation of the atypical and neurotoxic sphingoid metabolite 1-deoxy-sphinganine.
Catalog Number:
(89415-346)
Supplier:
Prosci
Description:
DRAK2 Antibody: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase-related apoptosis-inducing protein kinases). DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.
Catalog Number:
(103004-226)
Supplier:
Anaspec Inc
Description:
This serine substituted PLP (139-151) causes severe, acute experimental allergic encephalomyelitis in SJL mice.
Sequence: HSLGKWLGHPDKF MW: 1521.8 Da % Peak area by HPLC: 95 Storage condition: -20°C
Catalog Number:
(10355-310)
Supplier:
Bioss
Description:
Beta Arrestin 1 is a member of a family of proteins that are widely expressed but especially abundant in the central nervous system. Serving as an adaptor or scaffold molecule, beta Arrestin 1 is essential for mitogenic signaling. It mediates agonist dependent desensitization and internalization of G protein coupled receptors (GPCRs, e.g., beta 2 adrenergic receptor). After binding to their ligand and interacting with heterotrimeric G proteins, GPCRs are phosphorylated by G protein receptor kinases (GRKs) on serine residues. Beta Arrestin 1 has important roles in the cytoplasm and at the plasma membrane in the desensitization and internalization of G protein coupled receptors (GPCRs) and is increasingly appreciated to play an important role in the endocytosis and signaling of GPCRs. Beta Arrestin 1 in the cytosol is phosphorylated by ERK1 and 2 on serine 412 in a negative feedback mechanism and binds to the phosphorylated receptors at the plasma membrane. Serine 412 is then dephosphorylated and the GPCRs are internalized, leading to activation of the Ras, Raf, ERK1 and 2 signaling pathway.
Catalog Number:
(10279-436)
Supplier:
Bioss
Description:
The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. STK33 (serine/threonine kinase 33) is a 514 amino acid protein that belongs to the CaMK (calcium/calmodulin dependent kinase) subfamily of structurally related serine/threonine kinases. Widely expressed at low levels with predominant expression in testis, lung, retina and fetal organs such as brain, heart and spinal cord, STK33 contains one protein kinase domain and functions as a Ser/Thr protein kinase with a possible role in spermatogenesis. The gene encoding STK33 lies within a region on chromosome 11 that has been associated with a variety of defects, including Long QT syndrome, T-cell leukemia, Beckwith-Wiedemann syndrome, Usher syndrome 1C and various other malignancies.
Catalog Number:
(10472-870)
Supplier:
Bioss
Description:
SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.
Catalog Number:
(10749-406)
Supplier:
Prosci
Description:
DAPK2 Antibody: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as RIP and DAP kinase, are mediators of apoptosis. DAP kinase (DAPK) is pro-apoptotic calcium-regulated serine/threonine kinase containing death domain. Ectopic expression of DAPK induces cell death and suppresses oncogenic transformation. DAPK mediates IFNgamma; induced apoptosis. A novel DAP kinase-related protein was recently identified and designated DAPK2 and DRP-1. Ectopicly expressed DAPK2 induced apoptosis in various types of cells. DAPK has high sequence homology to ZIP kinase and DRAK1/2, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. The messenger RNA of DAPK2 is expressed in multiple human tissues.
Supplier:
Thermo Scientific Chemicals
Description:
1g CAS: 84311-18-2, MDL: MFCD02682596
Catalog Number:
(75791-438)
Supplier:
Prosci
Description:
Serpin B9 belongs to the large superfamily of serine proteinase inhibitors (serpins), which bind to and inactivate serine proteinases. Serpin B9 is an inhibitor of the granzyme B/perforin lytic pathway. It is expressed in normal mammary epithelial cells but not in most mammary carcinoma cell lines. These interactions are involved in many cellular processes, including coagulation, fibrinolysis, complement fixation, matrix remodeling, and apoptosis.
Catalog Number:
(10453-418)
Supplier:
Bioss
Description:
Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.
Catalog Number:
(10453-192)
Supplier:
Bioss
Description:
Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.
Catalog Number:
(10453-194)
Supplier:
Bioss
Description:
Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.
Catalog Number:
(10411-038)
Supplier:
Bioss
Description:
Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.
Catalog Number:
(77439-272)
Supplier:
Bioss
Description:
Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive.
Catalog Number:
(10081-570)
Supplier:
Proteintech
Description:
Integrin-linked kinase (ILK) is an ankyrin-repeat containing serine-threonine protein kinase capable of interacting with the cytoplasmic domains of integrin β1, β2, and β3 subunits and whose kinase activity is modulated by cell-extracellular matrix interactions. This protein belongs to the protein kinase superfamily. It can be autophosphorylated on serine residues.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
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