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Anti-SLC4A1 Rabbit Polyclonal Antibody

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PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activityThe protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.

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SFRS6 is involved in mRNA splicing and may play a role in the determination of alternative splicing. It belongs to the splicing factor SR family and has been shown to bind with and modulate another member of the family, SFRS12.The protein encoded by this gene is involved in mRNA splicing and may play a role in the determination of alternative splicing. The encoded nuclear protein belongs to the splicing factor SR family and has been shown to bind with and modulate another member of the family, SFRS12. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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Nop56p is a yeast nucleolar protein that is part of a complex with the nucleolar proteins Nop58p and fibrillarin. Nop56p is required for assembly of the 60S ribosomal subunit and is involved in pre-rRNA processing. NOL5A is similar in sequence to Nop56p and is also found in the nucleolus. Multiple transcript variants encoding several different isoforms have been found for this gene, but the full-length nature of most of them have not been determined.Nop56p is a yeast nucleolar protein that is part of a complex with the nucleolar proteins Nop58p and fibrillarin. Nop56p is required for assembly of the 60S ribosomal subunit and is involved in pre-rRNA processing. The protein encoded by this gene is similar in sequence to Nop56p and is also found in the nucleolus. Multiple transcript variants encoding several different isoforms have been found for this gene, but the full-length nature of most of them have not been determined.

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VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.

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Best known for their ability to conjugate glutathione (GSH) and thereby detoxify cellular environments, GSTs are also capable of binding nonsubstrate ligands with important cell signaling implications. GST is used as a purification tag for recombinant proteins.

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T-cell surface glycoprotein CD5 is also known as Lymphocyte antigen T1/Leu-1 and LEU1,which is phosphorylated on tyrosine residues by LYN,so CD5 can create binding sites for PTPN6/SHP-1.CD5 may act as a receptor in regulating T-cell proliferation. CD5 is expressed at various developmental and activation stages on human B cells.CD5 is a well established negative regulator of TCR and BCR signalling.CD5-positive cells may also prevent the emergence of autoimmunity by provision of cytokines such as IL-10. Development,selection and function of different B- and T-cell subsets or their preferential survival may be directly or indirectly dependent on different glycan structures associated with CD5 or CD5-like molecules.

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CD36 (Cluster of Differentiation 36) is also known as platelet membrane glycoprotein IV (GPIV), fatty acid translocase (FAT), thrombospondin receptor, collagen receptor, and scavenger receptor class B, member 3 (SRB3), is a member of the class B scavenger receptor family of cell surface proteins. The human CD36 gene encodes a single chain 472 amino acid residue protein containing both an N- and a C-terminal cytoplasmic tail and an extracellular loop.CD36 is found on platelets, erythrocytes, monocytes, differentiated adipocytes, mammary epithelial cells, spleen cells and some skin microdermal endothelial cells. CD36 is a multiligand pattern recognition receptor that interacts with a large number of structurally dissimilar ligands, including long chain fatty acid (LCFA), advanced glycation end products (AGE), thrombospondin-1, oxidized low-density lipoproteins (oxLDLs), high density lipoprotein (HDL), phosphatidylserine, apoptotic cells, beta-amyloid fibrils (fAβ), collagens I and IV, and Plasmodium falciparum infected erythrocytes. CD36 is required for the anti-angiogenic effects of thrombospondin1 In the corneal neovascularisation assay. On binding a ligand the protein and ligand are internalized. This internalisation is independent of macropinocytosis and occurs by an actin dependent mechanism requiring the activation Src-family kinases, JNK and Rho-family GTPases. CD36 ligands have also been shown to promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer.

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FUNCTION: Also acts as the receptor for echovirus 7 and related viruses (echoviruses 13, 21, 29 and 33).
SUBUNIT: Monomer (major form) and non-disulfide-linked, covalent homodimer (minor form).
PTM: The Ser/Thr-rich domain is heavily O-glycosylated.
SIMILARITY: Contains 4 Sushi (CCP/SCR) domains.
SUBCELLULAR LOCATION: Attached to the membrane by a GPI-anchor (isoform 2).
TISSUE SPECIFICITY: Expressed on the plasma membranes of all cell types that are in intimate contact with plasma complement proteins. It is also found on the surfaces of epithelial cells lining extracellular compartments, and variants of the molecule are present in body fluids and in extracellular matrix.

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Anti-TCOF1 Chicken Polyclonal Antibody

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The function remains unknown.

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Anti-POU3F2 Goat Polyclonal Antibody

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Anti-FANCM Goat Polyclonal Antibody

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Anti-POU3F3 Goat Polyclonal Antibody

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Anti-WFDC2 Goat Polyclonal Antibody

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Anti-GABRG2 Goat Polyclonal Antibody

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Mouse Complement C5 (C5a) is a glycoprotein that belongs to a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 77 amino acid peptide that is created by the C5a convertase proteolytic cleavage of C5 alphachain in the classical and alternative complement pathway (C4b2a3b, C3bBb3b). Mouse C5a has four alphahelices, plus three intra-chain disulfide bonds that form a triple loop structure. C5a functions via G-protein coupled receptor (GPCR) (C5aR/CD88). C5a is a potent chemoattractant and anaphylatoxin that acts on all classes of leukocytes and on many other cell types including endothelial, smooth muscle, kidney, liver, and neural cells. It mediates IL-8 release from bronchial epithelial cells. It also triggers an oxidative burst in macrophages and neutrophils, causing release of histamine in basophils and mast cells. C5a anaphylatoxin activity on hepatocytes results indirectly from interaction with nonparenchymal cell via prostanoid secretion. Mouse C5a shares 60% and 82% sequence identity to human and rat C5a, respectively.

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Interleukin-1 alpha (IL1 alpha) is a cytokine member of the interleukin-1 family. IL-1 consists of two distinct forms: IL1 alpha and IL1 beta that recognize the same cell surface receptors but are distinct proteins with approximately 25% amino acid sequence identity. IL1 alpha is constitutively produced by epithelial cells and plays an essential role in maintenance of skin barrier function. Upon stimulation, a wide variety of cells including osteoblasts, monocytes, macrophages can be induced to express IL1 alpha. IL1 alpha possesses a wide range of metabolic, physiological, haematopoietic activities, and is critically involved in the regulation of the immune responses and inflammatory responses.

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T-cell surface antigen CD2 is also known as Erythrocyte receptor, LFA-2, LFA-3 receptor, Rosette receptor, T-cell surface antigen T11/Leu-5 and SRBC, is a single-pass type I membrane protein found on the surface of T cells and natural killer (NK) cells. CD2 is a member of the immunoglobulin superfamily. CD2 / SRBC contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain. CD2 / SRBC interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3 / CD58) in humans, or CD48 in rodents, which are expressed on the surfaces of other cells. In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells. CD2 is a specific marker for T cells and NK cells, and can therefore be used in immunohistochemistry to identify the presence of such cells in tissue sections.

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Human recombinant SEMA4D (from HEK293 cells)

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Interleukin-2 receptor (IL-2R) is a heterotrimeric protein expressed on the surface of certain immune cells, such as lymphocytes, that binds and responds to a cytokine called IL-2. The IL-2R is made up of 3 subunits - α (CD25), β (CD122) and γ (CD132) - non-covalently associating. The α and β chains are involved in binding IL-2, while signal transduction following cytokine interaction is carried out by the γ-chain, along with the β subunit.
CD122 is also known as IL2R beta, is a member of the type I cytokine receptor family. CD122 is the receptor for interleukin-2 and is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2.

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Acetylcholinesterase is involved in termination of signal transmission at neuromuscular junctions. Differences in assembly and localization of the multiple synaptic forms of acetylcholinesterase are thought to arise through posttranscriptional events. The Yt erythrocyte blood group antigen system resides on the acetylcholinesterase molecule.

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Anti-DERL3 Rabbit Polyclonal Antibody

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Anti-SDCBP2 Goat Polyclonal Antibody

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Anti-BC035295 Goat Polyclonal Antibody

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Anti-MAL Goat Polyclonal Antibody

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Anti-UMOD Mouse Monoclonal Antibody

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Anti-TIMP2A Goat Polyclonal Antibody

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Anti-TIA1 Goat Polyclonal Antibody

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The function remains unknown.