Description: Recombinant E.Coli SecB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17.2 kDa. SecB was over-expressed in E. coli and purified by conventional chromatography.
Description: Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain having a molecular mass of 45 kDa.;Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.
Description: Protein CutA (CUTA) posseses a signal peptide and is widely expressed in brain. CUTA mayforms part of a complex of membrane proteins attached to acetylcholinesterase (AChE). CUTA takes part in cellular tolerance to a broad range of divalent cations other than copper. Alternate transcriptional splice variants, both protein-coding and non-protein-coding, have been found.
Description: FAM3C, also called interleukin-like EMT inducer, usually exist in most secretory epithelia. It belongs to the FAM3 family according to their sequence similarities. The up-regulation and/or mislocalization in breast cancer and liver carcinoma cells of FAM3C is strongly correlated with metastasis formation and survival. FAM3C can be involved in retinal laminar formation and promote epithelial to mesenchymal transition.
Description: Protein FAM3D is a novel cytokine-like protein that belongs to the FAM3 family. Human FAM3D is synthesized as a 224 amino acid precursor that contains a 25 amino acid signal sequence and a 199 amino acid mature chain. FAM3D is identified based on structural, but not sequence, homology to short chain cytokines including IL-2, IL-4 and GM-CSF. FAM3 proteins are four helix bundle cytokines with four conserved cysteines in all members (FAM3A-D). FAM3B is highly expressed in alpha and beta cells of the pancreas and is being investigated as a potential contributor to beta cell death and development of Type I Diabetes.
Description: Protein G is an immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria much like Protein A but with differing specificities. It is a 65-kDa (G148 protein G) and a 58 kDa (C40 protein G) cell surface protein that has found application in purifying antibodies through its binding to the Fc region. The native molecule also binds albumin, however, because serum albumin is a major contaminant of antibody sources, the albumin binding site has been removed from this recombinant form of Protein G.
Description: Protein L was isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind Ig(IgG,IgM,IgA,IgE and IgD) through L chain interaction, from which the name was suggested. Despite this wide-ranging binding capability with respect to Ig classes, Protein L is not a universal immunoglobilin-binding protein. Binding of Protein L to immunoglobulins is restricted to those containing kappa light chains (i.e., k chain of the VL domain). In humans and mice, kappa (k) light chains predominate. The remaining immunoglobulins have lambda (l) light chains. The recombinant protein contains four immunoglobulin (Ig) binding domains (Bdomains) of the native protein. Besides antibody, protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs).
Description: Myelin P2 Protein (PMP2) is a cytoplasmic protein which belongs to the Fatty-acid binding protein (FABP) family of calycin superfamily. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. PMP2 is found in peripheral nerve myelin and spinal cord myelin, the oligodendrocytes and Schwann cells, respectively. PMP2 may be involved in lipid transport protein in Schwann cells. It may decrease the inhibitory effect of T suppressors in the culture of immune lymph node cells.
Description: Human PAP, also known as 28 kDa heat- and acid-stable phosphoprotein, PDGF-associated protein, PDGFA-associated protein 1, PDAP1, HASPP28, is a protein which belongs to the PDAP1 family. The encoded protein in rodents has been shown to bind PDGFA with a low affinity. PDGF-Associated Protein (PAP) is a phosphoprotein that may enhance PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. PDAP1 expression is induced by TNF-alpha, and cells overexpressing PDAP1 show significantly less apoptosis on exposure to TNF-alpha.
Description: Myelin Protein P0 (MPZ) is a single-pass type I membrane glycoprotein which belongs to the myelin P0 protein family. MPZ contains one Ig-like V-type (immunoglobulin-like) domain, absent in the central nervous system. MPZ is a major component of the myelin sheath in peripheral nerves. It is postulated that MPZ is a structural element in the formation and stabilisation of peripheral nerve myelin, holding its characteristic coil structure together by the interaction of its positively-charged domain with acidic lipids in the cytoplasmic face of the opposed bilayer, and by interaction between hydrophobic globular of adjacent extracellular domains. Defects in MPZ associated with Charcot-Marie-Tooth disease and Dejerine-Sottas disease.
Description: Brevican Core Protein (BCAN) is a secreted protein that belongs to the aggrecan/versican proteoglycan family. BCAN contains one C-type lectin domain, one EGF-like domain, one Ig-like V-type domain, one Sushi (CCP/SCR) domain and two Link domains. BCAN may play a role in the terminally differentiating and the adult nervous system during postnatal development. BCAN could stabilize interactions between hyaluronan (HA) and brain proteoglycans.
Description: Probable serine carboxypeptidase CPVL, also known as Carboxypeptidase, vitellogenic-like, Vitellogenic carboxypeptidase-like protein, is a member of the peptidase S10 family. It is expressed in macrophages but not in other leukocytes. And specifically, it is abundantly expressed in heart and kidney, also expressed in spleen, leukocytes, and placenta. This enzyme may be involved in the digestion of phagocytosed particles in the lysosome, and also participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.
Description: Ubiquitin-Like-Conjugating Enzyme ATG3 (ATG3) is widely expressed and has highly levels in heart, skeletal muscle, kidney, liver and placenta. ATG3 as a E2-like enzyme, involves in autophagy and mitochondrial homeostasis. ATG3 catalyzes the conjugation of ATG8-like proteins to PE which is essential for autophagy. As an autocatalytic E2-like enzyme, ATG3 also can catalyzes the conjugation of ATG12 to itself which palys a role in mitochondrial homeostasis but not in autophagy.
Description: Ubiquitin-Like-Conjugating Enzyme ATG10 (ATG10) is a ubiquitous 28kDa member of the ATG10 family protein. ATG10 acts as an E2-like enzyme, catalyzes the transfer of ATG12 to ATG5 during in the initial stages of autophagesome formation. The heterodimer of ATG5 and ATG12 subsequntly associates non-covalently with an ATG16 multimer to generate an antophagosome. ATG10 plays a role in the conjugation of ATG12 to ATG5 by interaction with MAP1LC3A. In addition, ATG10 can diretly interact with ATG5 or ATG7.
Description: Toll-Interacting Protein (TOLLIP) is a member of the tollip family. TOLLIP localizes to the cytoplasm. It contains one C2 domain and one CUE domain. TOLLIP is an inhibitory adaptor protein for Toll-like receptors (TLR). The Toll-like receptors pathway is a part of the immune system that recognize structurally conserved molecular patterns of microbial pathogens, resulting in an inflammatory immune response. TOLLIP constitutes a complex with Tom1 to regulate endosomal transferring of ubiquitinated proteins. TOLLIP can negative regulate Toll-like receptors signaling, which may limit the production of proinflammatory mediators during the process of inflammation and infection.
Description: Cysteine Protease ATG4C (ATG4C) belongs to the peptidase C54 family. It is required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form which is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes. ATG4C is a cytoplasmic protein and high expressed in skeletal muscle, liver, testis and heart. ATG4C can be inhibited by N-ethylmaleimide.
Description: Galectin-Related Protein (LGALSL) is a 172 amino acid protein that contains one Galectin domain. LGALSL does not appear to bind carbohydrates or lactose as the critical residues required for binding are not conserved. LGALSL may play a significant role in stimulating smooth muscle growth in developing alveolar wall vessels and the development of pulmonary capillaries.
Description: Valosin-Containing Protein (VCP) is a nuclear protein that belongs to the AAA ATPase family. VCP is a putative ATP-binding protein involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. It is necessary for the fragmentation of Golgi stacks during mitosis and their reassembly after mitosis. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. VCP participates in the formation of the transitional endoplasmic reticulum (tER) and regulates E3 ubiquitin-protein ligase activity of RNF19A.
Description: Cytoplasmic Protein NCK1 (NCK1) is a cytoplasmic protein that contains one SH2 domain and three SH3 domains. NCK1 is a member of the adapter family, which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. NCK1 maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. NCK1 plays a role in the DNA damage response, but not in the detection of the damage by ATM/ATR. It is also involved in transducing signals from receptor tyrosine kinases to downstream signal recipients, such as ELK1-dependent transcriptional activation in response to activated Ras signaling.
Description: Cysteine Protease ATG4A (ATG4A) is a cytoplasmic protein that belongs to the peptidase C54 family. ATG4A is widely expressed in many tissues at a low level, but the highest expression is observed in skeletal muscle and brain. ATG4A is a cysteine protease required for autophagy; it cleaves the C-terminal part of MAP1LC3, GABARAPL2 or GABARAP. ATG4A is inhibited by N-ethylmaleimide. It is suggested that ATG4A has a significant role in suppressing various cancers.
Description: ATG5 is an E2 ubiquitin ligase which is necessary for autophagy. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity, dramatically highly expressed in apoptotic cells. It is activated by ATG7, conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate complex detaches from the membrane immediately before or after autophagosome formation is completed. ATG5 plays an important role in the apoptotic process, possibly within the modified cytoskeleton.
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