1103 Results for: "protein purification system"

Supplier: Proteintech

Kininogens are inhibitors of thiol proteases. Kininogen 1 plays important role in Kinin-kallikrein system. This gene is translated into High-molecular weight kininogen (HMWK) and low-molecular weight kininogen (LMWK) after alternative splicing. HMWK is produced by the liver together with prekallikrein. It acts mainly as a cofactor on coagulation and inflammation, and has no intrinsic catalytic activity. LMWK is produced locally by numerous tissues, and secreted together with tissue kallikrein. 11926-1-AP was generated against N-terminal 300 aa of HMW kininogen. It can bind both HMW and LMW kiniogen.

Supplier: Proteintech

HIP1 Belongs to the SLA2 family. HIP1 plays a role in clathrin-mediated endocytosis and trafficking. It is involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. It enhances androgen receptor (AR)-mediated transcription. HIP1 may act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. It binds 3-phosphoinositides (via ENTH domain). HIP1 may act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. HIP1 plays a functional role in the cell filament networks. It is required for differentiation, proliferation, and/or survival of somatic and germline progenitors. A chromosomal aberration involving HIP1 is found in a form of chronic myelomonocytic leukemia (CMML). The antibody is specific to HIP1.

Supplier: Proteintech

GRN, also known as PGRN or PCDGF, is a cysteine-rich protein of 68.5 kDa that is typically secreted into a highly glycosylated 88 kDa form. PGRN is a unique growth factor that plays an important role in cutaneous wound healing. It has an anti-inflammatory effect and promotes cell proliferation. When PCDGF is degraded to several 6–25 kDa fragments, called granulins (GRNs) by neutrophil proteases, a pro-inflammatory reaction occurs. PGRN is widely expressed, particularly in epithelial cells, immune cells, neurons, and chondrocytes. High levels of PGRN expression have been reported in human cancers, and its expression is closely correlated with the development and metastasis of several cancers. The recent discovery that mutations in the gene encoding for pro-granulin (GRN) cause frontotemporal lobar degeneration (FTLD), and other neurodegenerative diseases leading to dementia, has brought renewed interest in progranulin and its functions in the central nervous system.

Supplier: Proteintech

RGMA, also named as RGM, is a member of the repulsive guidance molecule (RGM) family that performs several functions in the developing and adult nervous system. It regulates cephalic neural tube closure, inhibits neurite outgrowth and cortical neuron branching, and the formation of mature synapses. RGMA binding to its receptor NEO1/neogenin induces activation of RHOA-ROCK1/Rho-kinase signaling pathway through UNC5B-ARHGEF12/LARG-PTK2 cascade, leading to collapse of the neuronal growth cone and neurite outgrowth inhibition. Furthermore, RGMA binding to NEO1/neogenin leads to HRAS inactivation by influencing HRAS1-PTK2-AKT1 pathway. It also functions as a bone morphogenetic protein (BMP) coreceptor that may signal through SMAD1, SMAD5, and SMAD8. RGMA is a molecular target for neuroprotection in retinal pathologies. the frequent genetic and epigenetic inactivation of RGMA in CRCs and adenomas along with its in vitro function collectively support its role as a tumor suppressor in colon cells.

Supplier: Bioss

Making up nearly 6% of the human genome, chromosome 6 contains around 1200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatibility complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf58 gene product has been provisionally designated C6orf58 pending further characterization.

Supplier: Proteintech

GFER(FAD-linked sulfhydryl oxidase) is also named as ALR, HERV1, HPO. It plays an important role in the disulfide relay system (DRS) in human mitochondria.The GFER gene codes for 2 distinct isoforms that are probably synthesized from the same mRNA with the use of different initiation codons. The long isoform (205 amino acids, 23 kD) is located mainly in the mitochondrial intermembrane space and exists under nonreducing and nondenaturing conditions as a homodimer and a heterodimer. The shorter isoform (125 amino acids, 15 kD), which lacks 80 amino acids at its N terminus compared to the longer isoform, is present predominantly in the nucleus.

Supplier: Proteintech

FXYD2 (FXYD domain-containing ion transport regulator 2), also known as the gamma-subunit of the NaK-ATPase, belongs to the FXYD family which has been proposed to be the regulators of Na, K-ATPase function by lowering affinities of the system for potassium and sodium. The expression of FXYD2 is most abundant in kidney, while it is also detected in several other tissues like placenta, pancreas, and dorsal root ganglia (DRGs). Three splice variants of FXYD2 have been reported in mouse kidney, namely FXYD2 γa, -γb,and -γc. FXYD2 γa has been identified as a pancreatic beta cell-specific biomarker. This antibody can recognize all three isoforms of FXYD2.

Supplier: Proteintech

IRF5, also named as SLEB10, contians one IRF tryptophan pentad repeat DNA-binding domain and belongs to the IRF family. It is a transcription factor involved in the induction of interferons IFNA and INFB and inflammatory cytokines upon virus infection. It is activated by TLR7 or TLR8 signaling. Genetic variations in IRF5 are associated with susceptibility to inflammatory bowel disease type 14 (IBD14) and systemic lupus erythematosus type 10 (SLEB10). IRF5 is also used as M1 marcrophage lineage marker. Alternative splice variant encoding different isoforms exist. Catalog#10547-1-AP is a rabbit polyclonal antibody raised against the C-terminal of human IRF5.

Supplier: Proteintech

HABP2 is also named as HGFAL, PHBP and belongs to the peptidase S1 family. It can activate coagulation factor VII and prourokinase and release the vasoactive peptide bradykinin by cleaving kininogen and is an important role in the regulation of the haemostasis system as well as fibroproliferative inflammatory processes . HABP2 is present as the 70 kDa inactive single chain precursor in human plasma and transforms to the active two chain form, 50 kDa heavy chain and 27 kDa light chain,and the 50 kDa heavy chain changes to two 26 kDa fragments, and 27 kDa light chain to 17 kDa and 8 kDa fragments, which are all bridged by disulfide linkages, by autocleavage.

Supplier: Bioss

Making up nearly 6% of the human genome, chromosome 6 contains around 1200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatibility complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf174 gene product has been provisionally designated C6orf174 pending further characterization.

Supplier: Proteintech

ATP6AP2, also named as ATP6IP2, CAPER, ELDF10, N14F, ATP6M8-9, Renin receptor and prorenin receptor, is believed to potentiate the renin–angiotensin system (RAS), conferring to prorenin, a likely pathological role at tissue level. The PRR has been identified in the microvascular endothelial cells of the retina, in which it seems to be involved in pathological neovascularization processes. The present study demonstrates for the first time that the PRR is expressed in human ATP6AP2 and suggests a molecular mechanism by which hypertension may exacerbate the pathology of dry AMD. ATP6AP2 functions as a renin and prorenin cellular receptor. It may mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS). Defects in ATP6AP2 are a cause of mental retardation X-linked with epilepsy (MRXE).

Supplier: Proteintech

CSPG4, also named as HMW-MAA, MCSP, MCSPG, MEL-CSPG, MSK16 and NG2, is a proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. CSPG4 may inhibit neurite outgrowth and growth cone collapse during axon regeneration. It is cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. CSPG4 may regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. It modulates the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. CSPG4 functions as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. It promotes retraction fiber formation and cell polarization through Rho GTPase activation and stimulates alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. CSPG4 activates FAK and ERK1/ERK2 signaling cascades. The antibody is specific to CSPG4.

Supplier: Proteintech

RNLS, also named as Renalase, C10orf59 and MAO-C, belongs to the renalase family. It is probable FAD-dependent amine oxidase secreted by the kidney, which circulates in blood and modulates cardiac function and systemic blood pressure. RNLS degrades catecholamines such as dopamine, norepinephrine and epinephrine in vitro. It lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis. RNLS has physiologically relevant catecholamine-oxidizing activity. This antibody is specific to RNLS.

Supplier: Proteintech

Estrogen receptor–binding fragment-associated antigen 9 (EBAG9) gene was identified as an estrogen-responsive gene. The gene product, receptor-binding cancer antigen expressed on SiSo cells (RCAS1), is associated with aggressive characteristics and poor overall survival for 15 different human malignancies. The correlation between RCAS1 expression and several clinicopathological variables, including tumor size, clinical stage, invasion depth and lymph node metastasis highlights this molecule's clinical significance. Expression of RCAS1 in tumor cells plays an important role in evasion from host immune system resulting tumor progression, invasion and metastasis. Further exploration of RCAS1 biological function will facilitate development of novel therapeutic strategies that target RCAS1.

Supplier: Proteintech

ATG5, also named as APG5L and ASP, belongs to the ATG5 family. It is required for autophagy. It plays an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles. It mediates autophagosome-independent host protection. This antibody is raised against 28-275 amino acids of human ATG5. It can recognize the ATG5-ATG12 complex (55 kDa) and free ATG5 (32 kDa).

Supplier: Proteintech

PMS2, also named as PMSL2, belongs to the DNA mismatch repair mutL/hexB family. It is a component of the post-replicative DNA mismatch repair system (MMR). It heterodimerizes with MLH1 to form MutL alpha. MulL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. It also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Defects in PMS2 are the cause of hereditary non-polyposis colorectal cancer type 4 (HNPCC4). Defects in PMS2 are a cause of mismatch repair cancer syndrome (MMRCS). This antibody is special to PMS2.

Supplier: Prosci

The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA3 is a protein similar to certain nuclear transport proteins of Xenopus and human. The predicted amino acid sequence shows similarity to Xenopus importin, yeast SRP1, and human RCH1 (KPNA2), respectively. The similarities among these proteins suggest that karyopherin alpha-3 may be involved in the nuclear transport system.The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA3, encodes a protein similar to certain nuclear transport proteins of Xenopus and human. The predicted amino acid sequence shows similarity to Xenopus importin, yeast SRP1, and human RCH1 (KPNA2), respectively. The similarities among these proteins suggests that karyopherin alpha-3 may be involved in the nuclear transport system. 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.

Supplier: Genetex

Myeloperoxidase is a hemoprotein that is abundantly expressed in neutrophils and secreted during their activation. Native Myeloperoxidase is represented as a covalently bound tetrameric complex of two glycosylated alpha chains (MW 59 - 64 kDa) and two unglycosylated beta chains (MW 14 kDa) with total MW 150 kDa and theoretical pI 9.2. Traditionally Myeloperoxidase was considered as a main target of anti-neutrophil cytoplasm antibodies (ANCA), the serological markers for certain systemic vasculities e.g. periarteriitis nodosa, microscopic polyarteriitis and pulmonary eosinophilic granulomatosis (Churg-Strauss syndrome). Low to moderate anti-Myeloperoxidase autoantibody levels are also reported in rheumatoid arthritis. Recently it was shown that Myeloperoxidase participates in the initiation and progression of cardiovascular disease. It possesses potent proinflammatory properties and may contribute directly to tissue injury. Now Myeloperoxidase is under consideration as one of the most promising cardiac markers.

Supplier: Genetex

Myeloperoxidase is a hemoprotein that is abundantly expressed in neutrophils and secreted during their activation. Native Myeloperoxidase is represented as a covalently bound tetrameric complex of two glycosylated alpha chains (MW 59 - 64 kDa) and two unglycosylated beta chains (MW 14 kDa) with total MW 150 kDa and theoretical pI 9.2. Traditionally Myeloperoxidase was considered as a main target of anti-neutrophil cytoplasm antibodies (ANCA), the serological markers for certain systemic vasculities e.g. periarteriitis nodosa, microscopic polyarteriitis and pulmonary eosinophilic granulomatosis (Churg-Strauss syndrome). Low to moderate anti-Myeloperoxidase autoantibody levels are also reported in rheumatoid arthritis. Recently it was shown that Myeloperoxidase participates in the initiation and progression of cardiovascular disease. It possesses potent proinflammatory properties and may contribute directly to tissue injury. Now Myeloperoxidase is under consideration as one of the most promising cardiac markers.

Supplier: Proteintech

Retinoid X receptor alpha (RXRA). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. This antibody is a rabbit polyclonal antibody raised against the 350 AA of human RXRA C-terminal. RXRA is highly expressed in liver, also expressed in lung, kidney and heart. It specifically recognizes the 51kd human RXRA protein.

Supplier: Proteintech

MLH1, also named as COCA2, belongs to the DNA mismatch repair mutL/hexB family. It heterodimerizes with PMS2 to form MutL alpha which is a component of the post-replicative DNA mismatch repair system (MMR). MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. MLH1 also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. MLH1 heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis. Defects in MLH1 are the cause of hereditary non-polyposis colorectal cancer type 2 (HNPCC2). Defects in MLH1 are a cause of mismatch repair cancer syndrome (MMRCS). Defects in MLH1 are a cause of Muir-Torre syndrome (MTS). Defects in MLH1 are a cause of susceptibility to endometrial cancer . This antibody is special to MLH1.

Supplier: Proteintech

In eukaryotic systems, the initiation of gene transcription involves the ordered assembly of a multiprotein complex on proximal promoter elements, consisting of RNA polymerase II and broad families of auxiliary transcription factors. Such factors can be divided into two major functional classes: the basal factors that are required for transcription of all Pol II genes, including TFIIA, B, D, E, F and H; and sequence specific factors that regulate gene expression. The basal transcription factors and Pol II form a specific multiprotein complex near the transcription start site by interacting with core promotor elements such as the TATA box generally located 25-30 base pairs upstream of the transcription start site. TFIIF, a heteromer composed of a small (RAP 30) and a large (RAP 74) subunit, acting at an intermediate stage in initiation complex formation, binds directly to RNA polymerase II in solution and decrease the affinity of RNA polymerase II for nonspecific DNA. In addition, TFIIF stimulates transcription elongation by RNA polymerase II.

Supplier: Proteintech

PAX8 is a member of the paired box (PAX) family of transcription factors, typically containing a paired box domain and a paired-type homeodomain. It is expressed during organogenesis of the thyroid gland, kidney and Mullerian system. It is thought to regulate the expression of Wilms tumor suppressor (WT1) gene and mutations in PAX8 have been associated with Wilms tumor cells, thyroid and ovarian carcinomas. PAX8 is a useful marker in distinguishing ovarian carcinomas from mammary carcinomas . PAX8 is expressed in a high percentage of ovarian serous, endometrioid, and clear cell carcinomas, but only rarely in primary ovarian mucinous adenocarcinomas.
PAX8 has 5 isoforms with calculated MW 31kd, 34kd, 41kd, 43kd and 48kd. And there is a 60kd band corresponding to the electrophoretic mobility of PAX8 . Proteintech’s 10336-1-AP antibody has cross-reactivities with the other PAX family members.

Supplier: Proteintech

Myelin/oligodendrocyte glycoprotein (MOG), a 26-to 28-kDa glycoprotein, a myelin antigen at the outer surface of the central nervous system (CNS) myelin sheath, which may trigger T-cell as well as B-cell responses. It therefore constitutes a pivotal target for autoimmune responses, which result in inflammation and also demyelination in the CNS. Its presence on the outer- most lamellae of mature CNS myelin and its late appearance during myelinogenesis suggest that it contributes to myelin maturation or maintenance. 10 isoforms of MOG produced by alternative splicing have been described, and heterodimers may be formed between the different isoforms. Defects in MOG are the cause of narcolepsy type 7 (NRCLP7), a neurological disabling sleep disorder characterized by excessive daytime sleepiness, sleep fragmentation, symptoms of abnormal rapid-eye-movement (REM) sleep, cataplexy, hypnagogic hallucinations, and sleep paralysis. Role of MOG in the pathogenesis of multiple sclerosis (MS) has been reported but remains to be clarified.

Supplier: Proteintech

Retinoid X receptor alpha (RXRA). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. This antibody is a rabbit polyclonal antibody raised against the 350 AA of human RXRA C-terminal. RXRA is highly expressed in liver, also expressed in lung, kidney and heart.

Supplier: Proteintech

Forkhead box A1(FOXA1),also named hepatocyte nuclear factor 3-alpha (HNF-3A), is a transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles (By similarity). Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally discribed as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: VWR International

VWR® 96 Sample Purification System is a high throughput, automated system that improves the efficiency and reproducibility of magnetic bead-based purification protocols.

Supplier: VWR International

VWR® 16 Sample purification system is a high throughput, automated system that improves the efficiency and reproducibility of magnetic bead-based purification protocols.