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Product Image-77001-228

DNA Clean and Concentrator™ Kits, Zymo Research

Supplier: Zymo Research
Description: Clean and concentrate up to 5 μg DNA with ≥6 μL elution in as little as 2 minutes with 0 μL wash residue carryover.

Image Unavailable-89350-850

Anti-MAPT Mouse Monoclonal Antibody [clone: TAU 2]

Catalog Number: (89350-850)
Supplier: Genetex
Description: 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.
Product Image-76020-604

RNA Clean & Concentrator™ Kits, Zymo Research

Supplier: Zymo Research
Description: The RNA Clean & Concentrator™ (RCC™) kits facilitate the efficient removal of RNA polymerases, ligases, and RNA modifying enzymes.

Product Image-10088-310

Anti-HLA-E Rabbit Polyclonal Antibody

Catalog Number: (10088-310)
Supplier: Proteintech
Description: Human major histocompatibility complex (MHC) antigens, also referred to as human leukocyte antigens (HLA), are encoded by genes located on the short arm of chromosome 6 (6p21.3). There are two classes of HLA antigens: class I and class II. This class I molecules are membrane glycoproteins composed of a heavy (alpha) chain which is encoded by a HLA class I gene, and β2-microglobulin light (beta) chain. The most extensively characterized members of the HLA class I gene family are the genes encoding the major transplantation antigenes, HLA-A, B and C. HLA-E is a non-classical MHC class I molecule.
Product Image-10672-014

Anti-RNF17 Rabbit Polyclonal Antibody

Catalog Number: (10672-014)
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. RNF17 (ring finger protein 17) or tudor domain-containing protein 4, TDRD4, SPATA23, Mmip-2 or FLJ11045, is a testis-specific protein and and novel key regulator of spermiogenesis containing 1,623 amino acids. By distributing Mad proteins to the cytoplasm, RNF17 regulates the transcriptional activity of c-Myc. Although showing localization in the nucleus, RNF17 is predominantly observed in cytoplasm and is a component of a novel nuage found in male germ cells. The gene encoding RNF17 maps to human chromosome 13q12.12 and encodes one RING-type zinc finger and four tudor domains. As a result of alternative splice events, five RNF17 isoforms exisit.
Image Unavailable-10092-412

Anti-PLA2G12A Rabbit Polyclonal Antibody

Catalog Number: (10092-412)
Supplier: Proteintech
Description: PLA2G12A (or PLA2G12) gene encodes group XII secreted phospholipase A2 (sPLA2) which catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Cellular arachidonate (AA) release and prostaglandin (PG) production is regulated by sPLA(2)s, groups III and XII. Group XII sPLA2 have relatively low specific activity and are structurally and functionally distinct from other sPLA2s. Cells transfected with group XII sPLA(2) exhibited abnormal morphology, suggesting a unique functional aspect of this enzyme. Role of sPLA2s as potential tumour biomarkers and therapeutic targets for various cancers have been reported.
Product Image-10822-216

Mouse Recombinant IL-27/P28 (from E. coli)

Catalog Number: (10822-216)
Supplier: FUJIFILM IRVINE SCIENTIFIC, INC
Description: The p28 subunit of interleukin 27 (IL-27), also known as interleukin 30 (IL-30), is a member of the interleukin 12 (IL-12) family of cytokines. p28 is a secreted polypeptide that associates with the Epstein-Barr virus induced gene 3 (EBI3) to form the IL-27 cytokine heterodimer complex. IL-27 functions as a proinflammatory cytokine that induces immunomodulatory effects in naïve CD4+ T cells, mast cells, and monocytes. p28 can also form a complex with cytokine-like factor 1 (CLF), that is secreted by dendritic cells, to regulate natural killer (NK) and T cell functions.
Image Unavailable-89350-852

Anti-MAPT Mouse Monoclonal Antibody [clone: TAU 2]

Catalog Number: (89350-852)
Supplier: Genetex
Description: 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.
Image Unavailable-89359-344

Anti-MAPT Mouse Monoclonal Antibody [clone: TAU 2]

Catalog Number: (89359-344)
Supplier: Genetex
Description: 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.
Image Unavailable-TCA0528-025G

L-Arginine hydrochloride ≥98.0% (by HPLC, titration analysis)

Supplier: TCI America
Description: CAS Number: 1119-34-2
MDL Number: MFCD00064550
Molecular Formula: C6H14N4O2
Molecular Weight: 210.66
Purity/Analysis Method: >98.0% (HPLC,T)
Form: Crystal
Melting point (°C): 235
Specific rotation [a]20/D: 23 deg (C=8, HCl(1+1))

SDS Certificates

Product Image-10088-334

Anti-HMGB1 Rabbit Polyclonal Antibody

Catalog Number: (10088-334)
Supplier: Proteintech
Description: The HMG (high mobility group) proteins are nonhistone chromosomal proteins that is present in almost all eukaryotic cells, and it functions to stabilize NUCLEOSOME formation and acts as a transcription-factor-like protein that regulates the expression of several genes. Once injury, infection or other inflammatory stimuli, activated macrophages, mature dendritic cells and natural killer cells can secret HMGB1, which act as a crucial cytokine. HMGB1 also involved in V(D)J recombination by acting as a cofactor of the RAG complex, stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Act as a Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells. HMGB1 (high mobility group box 1) modulates gene expression in the nucleus, but certain immune cells secrete HMGB1 as an extracellular Alarmin to signal tissue damage.The nuclear HMGB1 relocalizes to the extracellular milieu in senescent human and mouse cells in culture and in vivo, which stimulated cytokine secretion through TLR-4 signaling (23649808).This antibody is a rabbit polyclonal antibody raised against full length HMGB1 of human origin.
Product Image-77001-116

Zymoclean™ Gel DNA Recovery Kits, Zymo Research

Supplier: Zymo Research
Description: The Zymoclean Gel DNA Recovery Kits provide for the rapid purification of high quality DNA from TAE/TBE-bufffered agarose gels.

Product Image-10082-818

Anti-ALPL Rabbit Polyclonal Antibody

Catalog Number: (10082-818)
Supplier: Proteintech
Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. ALPL(Alkaline phosphatase, tissue-nonspecific isozyme) is also named as AP-TNAP, TNSALP and belongs to the alkaline phosphatase family. It can exsit as a homodimer with the molecular weight of 140 kDa. ALPL was synthesized as a 66-kDa endo-b-N-acetylglucos-aminidase H (Endo H)-sensitive form, and processed to an 80-kDa mature form, which is anchored to the plasma membrane via glycosylphosphatidylinositol (GPI).This antibody can bind the four mentioned alkaline phosphatases.
Product Image-10750-158

Anti-RGPD5 Rabbit Polyclonal Antibody

Catalog Number: (10750-158)
Supplier: Prosci
Description: RGPD5 Antibody: The RANBP2-like and GRIP domain containing 5 protein (RGPD5) has high similarity to RANBP2, a large RAN-binding protein localized at the cytoplasmic side of the nuclear pore complex. The gene coding for RGPD5 is thought to have arisen from a gene duplication event of RANBP2 as these highly homologous genes are located close to each other at chromosome 2q11-q12. RGPD5 was identified as an HIV dependency factor (HDF), suggesting that RGPD5 may be an important drug target in HIV treatment. At least two isoforms of RGPD5 are known to exist, of which the shorter isoform is expressed primarily in testis, while the longer of the two is expressed at low levels in a number of somatic tissues.
Product Image-89416-268

Anti-HAP1 Rabbit Polyclonal Antibody

Catalog Number: (89416-268)
Supplier: Prosci
Description: HAP1 Antibody: Huntington's disease (HD), a neurodegenerative disorder characterized by loss of striatal neurons, is caused by an expansion of a polyglutamine tract in the HD protein huntingtin. HAP1 was initially identified through a two-hybrid library screening; the binding of HAP1 to huntingtin correlated with the expansion of the polyglutamine tract. HAP1 also interacts with two cytoskeletal proteins (dynactin and pericentriolar autoantigen protein 1), suggesting that HAP1 may play a role in vesicular trafficking or organelle transport. HAP1 is also involved with the huntingtin-enhanced BDNF transport along the cellular microtubles. Attenuation of this process led to the loss of neurotrophic support and neuronal toxicity, which suggests that loss of this function might contribute to pathogenesis. Several alternatively spliced isoforms have been described for HAP1.
Product Image-10791-630

VWR® Reach-In Refrigerators with Solid Doors and Natural Refrigerant

Catalog Number: (10791-630)
Supplier: VWR International
Description: Units feature a stainless steel front exterior with white aluminum interior and stainless steel floor.

UL Listed Environmentally Preferable cUL Listed Product available on GSA Advantage®


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