You Searched For: N-Cbz-L-serine


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Catalog Number: (89279-172)
Supplier: Genetex
Description: Rabbit polyclonal to DRAK2


Catalog Number: (10108-114)
Supplier: Prosci
Description: SARS belongs to the class II amino-acyl tRNA family. The enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.


Catalog Number: (10108-116)
Supplier: Prosci
Description: SARS belongs to the class II amino-acyl tRNA family. The enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.


Catalog Number: (89320-726)
Supplier: Genetex
Description: Rabbit Polyclonal antibody to PASK (PAS domain containing serine/threonine kinase)


Supplier: MilliporeSigma
Description: Proteinase K is a highly active 28,904-Da serine protease isolated from the fungus Tritirachium album
Catalog Number: (76119-982)
Supplier: Bioss
Description: Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines.


Catalog Number: (10472-772)
Supplier: Bioss
Description: PLK5 (Serine/threonine-protein kinase PLK5) belongs to the protein kinase superfamily and Ser/Thr protein kinase family and CDC5/Polo subfamily. PLK5P contains 1 POLO box domain and 1 Serine/Threonine protein kinase catalytic domain.


Catalog Number: (10472-782)
Supplier: Bioss
Description: PLK5 (Serine/threonine-protein kinase PLK5) belongs to the protein kinase superfamily and Ser/Thr protein kinase family and CDC5/Polo subfamily. PLK5P contains 1 POLO box domain and 1 Serine/Threonine protein kinase catalytic domain.


Catalog Number: (10495-112)
Supplier: Bioss
Description: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression.


Catalog Number: (89165-658)
Supplier: Enzo Life Sciences
Description: A ketoaldehyde. An excellent inhibitor of the chymotrypsin-like activity of the proteasome and serine and cysteine proteases in general.


Supplier: MilliporeSigma
Description: Irreversible inhibitor of serine proteases. Its mechanism of action is analogous to that of diisopropylfluorophosphate. PMSF causes sulfonylation of the active-site serine residues. Also reported to inhibit internucleosomal DNA fragmentation in immature thymocytes. Effective concentration: 50µM.
Catalog Number: (77561-050)
Supplier: Sino Biological
Description: The 10 amino acids of PAKtide peptide (RRRLSFAEPG) contain a serine/threonine protein kinase phosphorylation site in a common seven-residue epitope (1, 2).

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Catalog Number: (75791-692)
Supplier: Prosci
Description: Activin Receptor-Like Kinase 1 (ALK-1) is a type I cell-surface receptor for the TGF- beta superfamily of ligands, which mediates signaling of BMP9 (bone morphogenetic protein) and BMP10. ALK1 signaling is necessary for angiogenesis during embryogenesis, wound healing, and tumor growth. ALK-1 has a high degree of similarity in serine-threonine kinase subdomains, a glycine and serine rich region preceding the kinase-domain, and a C-terminal tail with other activin receptor-like kinase proteins. ALK-1 is mainly expressed in endothelial cells regulating proliferation and migration in vitro and angiogenesis in vivo. Mutations in ALK-1 as well as in endoglin are associated with hereditary hemorrhagic telangiectasia (HHT), suggesting ALK-1 plays a critical role for in the control of blood vessel development or repair.


Catalog Number: (75789-588)
Supplier: Prosci
Description: Tryptases are Trypsin-like Serine Proteases


Catalog Number: (10464-150)
Supplier: Bioss
Description: May modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues.Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site. SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted protein which belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, or small molecule agents may be the link to drug discovery and development.


Catalog Number: (10338-778)
Supplier: Bioss
Description: p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.


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