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2-Amino-2,3-dimethylbutyramide
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2-Amino-2,3-dimethylbutyramide
Catalog Number:
(10278-176)
Supplier:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.
Catalog Number:
(10278-174)
Supplier:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.
Catalog Number:
(10278-226)
Supplier:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. LRRC23 (leucine-rich repeat-containing protein 23), also known as leucine-rich protein B7, is a 343 amino acid protein that contains eight LRR (leucine-rich) repeasts and one LRRCT domain. LRRC23 exists as two alternatively spliced isoforms and is encoded by a gene mapping to chromosome 12.
Catalog Number:
(75789-374)
Supplier:
Prosci
Description:
The human Polymeric Immunoglobulin Receptor (pIgR) is a 100 kDa type I transmembrane glycoprotein. Its precursor is 764 amino acids. It contains an 18 amino acid signal sequence, a 620 amino acid extracellular region, a 23 amino acid transmembrane fragment, and a 103 amino acid cytoplasmic domain. pIgR is synthesized by secretory epithelial cells with five Ig-like domains in extracellular region, and transfer to the basolateral plasma membrane. For IgA and IgM polymers, in addition to alpha-heavy chains and light Ig chains, a short polypeptide named joining chain (J chain) is also contained and required. pIgR can bind larger polymers of IgA (pIgA) and pentameric IgM as a carrier that transports IgA and IgM across epithelium. The receptor-ligand complexes are endocytosed and transcytosed to the apical surface, then proteolytic cleavage of the sixth extracellular domain of pIgR and generate secretory IgA (SIgA), the pIgR fragment is referred to as secretory component (SC). SIgA is a important component of the mucosal immune system. SC is anti-microbial properties and protects SIgA from proteolytic degradation
Catalog Number:
(103670-154)
Supplier:
Sino Biological
Description:
A DNA sequence encoding the mature form of Cynomolgus (<i>Macaca fascicularis</i>) CXCL13 (Val 23-Pro 109) was expressed, with an N-terminal polyhistidine tag.
Supplier:
PeproTech, Inc.
Description:
BMPs (Bone Morphogenetic Proteins) belong to the TGF-β superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 plays an important role in cardiac morphogenesis, and is expressed in a variety of tissues, including lung, spleen, brain, liver, prostate ovary and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant Human BMP-2 is a 26.0 kDa homodimeric protein consisting of two 115 amino acid polypeptide chains. Manufactured using all Animal-Free reagents.
Catalog Number:
(10669-742)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Catalog Number:
(10669-740)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Catalog Number:
(EM8.07340.0005)
Catalog Number:
(10751-600)
Supplier:
Prosci
Description:
VKORC1 Antibody: Vitamin K epoxide reductase complex subunit 1 (VKORC1) is the enzyme that is responsible for reducing vitamin K 2,3-epoxide to the enzymatically activated form which is essential for blood clotting. This enzymatically activated form of vitamin K is a reduced form required for the carboxylation of glutamic acid residues in some blood-clotting proteins. Fatal bleeding can be caused by vitamin K deficiency and by the vitamin K antagonist warfarin, and it is VKORC1 that is sensitive to warfarin. In humans, mutations in this gene can be associated with deficiencies in vitamin-K-dependent clotting factors and, in humans and rats, with warfarin resistance.
Catalog Number:
(10669-724)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Catalog Number:
(10669-738)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Supplier:
Prosci
Description:
FGF-acidic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors. Recombinant murine FGF-acidic is a 15.9 kDa protein consisting of 141 amino acid residues.
Catalog Number:
(76010-996)
Supplier:
Prosci
Description:
2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. This gene encodes a multifunctional enzyme that catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. The enzyme also has phosphoglycerate phosphomutase activity. Deficiency of this enzyme increases the affinity of cells for oxygen. Mutations in this gene result in hemolytic anemia. Multiple alternatively spliced variants, encoding the same protein, have been identified.
Catalog Number:
(10801-624)
Supplier:
Rockland Immunochemical
Description:
Gelsolin, a protein of leukocytes, platelets, and other cells, severs actin filaments in the presence of submicromolar calcium, thereby solating cytoplasmic actin gels. A gelsolin variant with 23 more N-terminal amino acids is a plasma component probably involved in the clearance of actin, the most abundant human protein, from the circulation. Gelsolin is located in 9q34. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. This antibody is suitable for researchers interested in cell research and cytoskeletal signaling research.
Catalog Number:
(10669-736)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
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