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Catalog Number: (10782-106)

Supplier: Biosensis

Description: Microtubules are 25nm diameter protein rods found in most kinds of eukaryotic cells. They are polymerized from a dimeric subunit made of one 'a' subunit and one 'b' tubulin subunit. Microtubules are associated with a family of proteins called microtubule associated proteins (MAPs), which includes the protein t (tau) and a group of proteins referred to as MAP1, MAP2, MAP3, MAP4 and MAP5. MAP2 is made up of two ~280kDa apparent molecular weight bands referred to as MAP2 a and MAP2 b. A third lower molecular weight form, usually called MAP2c, corresponds to a pair of protein bands running at ~70kDa on SDS-PAGE gels. All these MAP2 forms are derived from a single gene by alternate transcription, and all share a C-terminal sequence which includes either three or four microtubule binding peptide sequences, which are very similar to those found in the related microtubule binding protein t (tau). MAP2 isoforms are expressed only in neuronal cells and specifically in the perikarya and dendrites of these cells. Antibodies to MAP2 are therefore excellent markers on neuronal cells, their perikarya and neuronal dendrites.

Catalog Number: (10424-956)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (76081-284)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (10424-960)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (10424-770)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (10424-784)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (76081-282)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier: TMW Media Group

Description: Sharpen basic geography skills.

Catalog Number: (10424-958)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (10424-782)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (10488-152)

Supplier: Bioss

Description: Acyl-coenzyme A synthetases (ACSs) are a large family of related enzymes known to catalyze the fundamental initial reaction in fatty acid metabolism. The ACS family is roughly characterized based on fatty acid chain length preference amongst different members. The nomenclature in the ACS family reflects this relationship and includes short-chain ACS (ACSS), medium-chain ACS (ACSM), long-chain ACS (ACSL) and very long-chain ACS (ACSVL). ACSVL family members are capable of activating both long (LCFAs) and very long-chain fatty acids (VLCFAs). There are six members of the human ACSVL subfamily, which have been described as solute carrier family 27A (SLC27A) gene products. They represent a group of evolutionarily conserved fatty acid transport proteins (FATPs) recognized for their role in facilitating translocation of long-chain fatty acids across the plasma membrane. The family nomenclature has recently been unified with their respective acyl-CoA synthetase family designations: ACSVL1 (FATP2), ACSVL2 (FATP6), ACSVL3 (FATP3), ACSVL4 (FATP1), ACSVL5 (FATP4) and ACSVL6 (FATP5). ACSVLs have unique expression patterns and are found in major organs of fatty acid metabolism, such as adipose tissue, liver, heart and kidney. ACSVL2 is a 619 amino acid multi-pass membrane protein. Encoded by a gene that maps to human chromosome 5q23.3, ACSVL2 may function as the predominant fatty acid protein transporter in heart.

Catalog Number: (10424-786)

Supplier: Bioss

Description: ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Catalog Number: (77439-890)

Supplier: Bioss

Description: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'.

Catalog Number: (10488-164)

Supplier: Bioss

Description: Acyl-coenzyme A synthetases (ACSs) are a large family of related enzymes known to catalyze the fundamental initial reaction in fatty acid metabolism. The ACS family is roughly characterized based on fatty acid chain length preference amongst different members. The nomenclature in the ACS family reflects this relationship and includes short-chain ACS (ACSS), medium-chain ACS (ACSM), long-chain ACS (ACSL) and very long-chain ACS (ACSVL). ACSVL family members are capable of activating both long (LCFAs) and very long-chain fatty acids (VLCFAs). There are six members of the human ACSVL subfamily, which have been described as solute carrier family 27A (SLC27A) gene products. They represent a group of evolutionarily conserved fatty acid transport proteins (FATPs) recognized for their role in facilitating translocation of long-chain fatty acids across the plasma membrane. The family nomenclature has recently been unified with their respective acyl-CoA synthetase family designations: ACSVL1 (FATP2), ACSVL2 (FATP6), ACSVL3 (FATP3), ACSVL4 (FATP1), ACSVL5 (FATP4) and ACSVL6 (FATP5). ACSVLs have unique expression patterns and are found in major organs of fatty acid metabolism, such as adipose tissue, liver, heart and kidney. ACSVL2 is a 619 amino acid multi-pass membrane protein. Encoded by a gene that maps to human chromosome 5q23.3, ACSVL2 may function as the predominant fatty acid protein transporter in heart.

Catalog Number: (10490-080)

Supplier: Bioss

Description: Acyl-coenzyme A synthetases (ACSs) are a large family of related enzymes known to catalyze the fundamental initial reaction in fatty acid metabolism. The ACS family is roughly characterized based on fatty acid chain length preference amongst different members. The nomenclature in the ACS family reflects this relationship and includes short-chain ACS (ACSS), medium-chain ACS (ACSM), long-chain ACS (ACSL) and very long-chain ACS (ACSVL). ACSVL family members are capable of activating both long (LCFAs) and very long-chain fatty acids (VLCFAs). There are six members of the human ACSVL subfamily, which have been described as solute carrier family 27A (SLC27A) gene products. They represent a group of evolutionarily conserved fatty acid transport proteins (FATPs) recognized for their role in facilitating translocation of long-chain fatty acids across the plasma membrane. The family nomenclature has recently been unified with their respective acyl-CoA synthetase family designations: ACSVL1 (FATP2), ACSVL2 (FATP6), ACSVL3 (FATP3), ACSVL4 (FATP1), ACSVL5 (FATP4) and ACSVL6 (FATP5). ACSVLs have unique expression patterns and are found in major organs of fatty acid metabolism, such as adipose tissue, liver, heart and kidney. ACSVL2 is a 619 amino acid multi-pass membrane protein. Encoded by a gene that maps to human chromosome 5q23.3, ACSVL2 may function as the predominant fatty acid protein transporter in heart.

Catalog Number: (10490-084)

Supplier: Bioss

Description: Acyl-coenzyme A synthetases (ACSs) are a large family of related enzymes known to catalyze the fundamental initial reaction in fatty acid metabolism. The ACS family is roughly characterized based on fatty acid chain length preference amongst different members. The nomenclature in the ACS family reflects this relationship and includes short-chain ACS (ACSS), medium-chain ACS (ACSM), long-chain ACS (ACSL) and very long-chain ACS (ACSVL). ACSVL family members are capable of activating both long (LCFAs) and very long-chain fatty acids (VLCFAs). There are six members of the human ACSVL subfamily, which have been described as solute carrier family 27A (SLC27A) gene products. They represent a group of evolutionarily conserved fatty acid transport proteins (FATPs) recognized for their role in facilitating translocation of long-chain fatty acids across the plasma membrane. The family nomenclature has recently been unified with their respective acyl-CoA synthetase family designations: ACSVL1 (FATP2), ACSVL2 (FATP6), ACSVL3 (FATP3), ACSVL4 (FATP1), ACSVL5 (FATP4) and ACSVL6 (FATP5). ACSVLs have unique expression patterns and are found in major organs of fatty acid metabolism, such as adipose tissue, liver, heart and kidney. ACSVL2 is a 619 amino acid multi-pass membrane protein. Encoded by a gene that maps to human chromosome 5q23.3, ACSVL2 may function as the predominant fatty acid protein transporter in heart.