((Difluoromethyl)sulfonyl)benzene
Supplier:
MP Biomedicals
Description:
Storage: -20 °C.
Adenosine 5'-triphosphate (ATP) and its phosphate bonds are the basic components of energy exchange in many biological systems. Adenosine 5'-triphosphate (ATP) is a central component of energy storage and metabolism in vivo. ATP is used in many cellular processes, respiration, biosynthetic reactions, motility, and cell division. ATP is a substrate of many kinases involved in cell signaling and of adenylate cyclase(s) that produce the second messenger cAMP. ATP provides the metabolic energy to drive metabolic pumps. ATP serves as a coenzyme in a wide array of enzymatic reactions. P2 purinergic agonist; increases activity of Ca2+-activated K+ channels; substrate for ATP-dependent enzyme systems.
Catalog Number:
(10259-748)
Supplier:
Bioss
Description:
ATP13A2 is a 1,180 amino acid multi-pass membrane protein that belongs to the P5 subfamily of ATPases which play an important role in the transportation of inorganic cations. Expressed as multiple alternative spliced isoforms, ATP13A2 functions to catalyze the conversion of ATP to ADP and a free phosphate, thereby participating in the active transport of ions across cellular membranes. Defects in the gene encoding ATP13A2 are the cause of Kufor-Rakeb syndrome (KRS), a rare hereditary type of Parkinson’s disease that exhibits juvenile onset and is characterized by neurodegeneration and dementia. The ATP13A2 gene maps to human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome.
Catalog Number:
(10263-998)
Supplier:
Bioss
Description:
The Huntingtin protein contains a polyglutamine region, which leads to Huntingtin’s disease (HD) when the number of glutamine repeats exceeds thirty-five. The mutated Huntingtin protein acts within the nucleus to induce neurodegeneration by a cell-specific apoptotic mechanism. The loss of activity of the Huntingtin protein may be contributed to abnormal interactions between the mutant protein and other associated cellular proteins. Huntingtin interacts with a variety of proteins including HAP1, glyceraldehyde phosphate dehydrogenase (GAPDH), HAP40, Rab5 and HIP1. HAP40 mediates the recruitment of Huntingtin by Rab5 onto early endosomes. Specifically, this complex regulates endosome motility, which may be a key event of the pathogenetic process leading to neurodegeneration in HD.
Catalog Number:
(10108-810)
Supplier:
Prosci
Description:
EDG8 is a receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. It Is coupled to both the G (i/0)alpha and G (12) subclass of heteromeric G-proteins (By similarity). It may play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms.
Supplier:
PeproTech, Inc.
Description:
The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-II is 7.5 kDa.
Catalog Number:
(10239-798)
Supplier:
Bioss
Description:
Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling.
Catalog Number:
(75842-508)
Supplier:
BIOGEMS INTERNATIONAL INC.
Description:
The LN3 monoclonal antibody specifically reacts with the human leukocyte antigen-DR (HLA-DR), a MHC class II heterodimeric surface glycoprotein. HLA-DR is expressed on the antigen presenting surfaces of monocytes, macrophages, dendritic cells, activated T cells, and B cells. It is integral to peptide presentation to CD4+ T cells.
Supplier:
Prosci
Description:
The IGFs are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar by structure and function to insulin, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds.
Catalog Number:
(75843-520)
Supplier:
BIOGEMS INTERNATIONAL INC.
Description:
The 11B11 monoclonal antibody specifically reacts with mouse 14 kDa cytokine IL-4, expressed by the activated NKT cells and mast cells. IL-4 is species-specific and stimulates the proliferation and differentiation of B lymphocytes. It upregulates the expression of IgE receptors and class II MHC antigen.The 11B11 antibody neutralizes the IL-4 cytokine.
Catalog Number:
(10450-448)
Supplier:
Bioss
Description:
Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
Catalog Number:
(10450-446)
Supplier:
Bioss
Description:
Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
Catalog Number:
(10450-442)
Supplier:
Bioss
Description:
Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
Catalog Number:
(10450-454)
Supplier:
Bioss
Description:
Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
Catalog Number:
(76202-242)
Supplier:
Enzo Life Sciences
Description:
Produced in <i>E. coli.</i> A non-glycosylated protein containing 137 amino acids.
Catalog Number:
(10391-274)
Supplier:
Bioss
Description:
The hexokinases utilize Mg-ATP as a phosphoryl donor to catalyze the first step of intracellular glucose metabolism, the conversion of glucose to glucose-6-phosphate. Four hexokinase isoenzymes have been identified, including hexokinase I (HXK I), hexokinase II (HXK II), hexokinase III (HXK III) and hexokinase IV (HXK IV, also designated glucokinase or GCK). Hexokinases I-III each contain an N-terminal cluster of hydrophobic amino acids. Glucokinase lacks the N-terminal hydrophobic cluster. The hydrophobic cluster is thought to be necessary for membrane binding. This is substantiated by the finding that glucokinase has lower affinity for glucose than do the other hexokinases. HXK I has been shown to be expressed in brain, kidney and heart tissues as well as in hepatoma cell lines. HXK II is involved in the uptake and utilization of glucose by adipose and skeletal tissues. Of the hexokinases, HXK III has the highest affinity for glucose. Glucokinase is expressed in pancreatic beta cells where it functions as a glucose sensor, determining the “set point†for insulin secretion.
Catalog Number:
(10072-440)
Supplier:
Prosci
Description:
The IGFs are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar by structure and function to insulin, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant murine IGF-I is a 7.6 kDa globular protein containing amino acids including 3 intra-molecular disulfide bonds.
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