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Product Image-470200-342

Hydrion Test Paper Strips

Supplier: Micro Essential
Description: Use Hydrion A to test in the range of 2-4-6-8-10 and Hydrion B for the range of 1-3-5-7-9-11. Both strips let you test the pH scale in 2.0 units.<BR>Includes: color chart.

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-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.
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.
Product Image-470201-938

Immersion Oil, Type A

Catalog Number: (470201-938)
Supplier: Cargille Laboratories
Description: Essential for Sharp Resolution at High Magnification

SDS


Image Unavailable-75810-820

L(+)-Cysteine hydrochloride monohydrate 98,0 FCC

Catalog Number: (75810-820)
Supplier: Spectrum Chemicals
Description: L-Cysteine Monohydrochloride, Monohydrate, FCC - The FCC grade meets the requirements of the Food Chemical Codex indicates and is suitable for all food, beverage and nutritional supplement applications. Spectrum Chemical offers over 300 Food grade chemical ingredients packaged in laboratory size bottles to production drum quantities and are manufactured, packaged and stored under current Good Manufacturing Practices (cGMP) per 21CFR part 211 in FDA registered and inspected facilities.
Product Image-10806-344

VWR® Rainin® Micro Hook

Catalog Number: (10806-344)
Supplier: VWR International
Description: The VWR® Rainin Micro Hook is constructed from German steel, and features a blunt tip.
Product Image-17477-020

VWR® Micro Burets, Class A

Catalog Number: (17477-020)
Supplier: VWR International
Description: Borosilicate glass buret manufactured to Class A specifications for burets.
Product Image-89038-526

VWR® Natural Gas Micro Burner

Catalog Number: (89038-526)
Supplier: VWR International
Description: Micro burner with flame stabilizer provides an intense small flame suitable for micro procedures and analyses.

Certificates


Product Image-10806-340

VWR® Graefe Micro Hook

Supplier: VWR International
Description: The VWR® Graefe Micro Hook is constructed from German steel.

Product Image-10806-338

VWR® Bowman Micro Needle

Supplier: VWR International
Description: The VWR® Bowman Micro Needle is constructed from German steel.

Product Image-10032-324

VWR® Micro Homogenizing Packages

Supplier: VWR International
Description: The VWR® Standard Micro-Homogenizing Package fits into 500µL, 1.5 mL, and 2 mL micro-tubes.

Product Image-76457-360

VWR® Premium Vannas Micro Dissecting Scissors

Supplier: VWR International
Description: These spring-action micro dissecting scissors are perfect for micro dissecting applications.

Product Image-80094-500

VWR® Micro Incinerator

Catalog Number: (80094-500)
Supplier: VWR International
Description: VWR® Micro Incinerator is designed to sterilize metal inoculating loops and needles without using an open flame; eliminating aerosoling of microorganisms.

Small Business Enterprise


Product Image-76533-876

VWR® Micro Star 21 and 21R Microcentrifuges

Supplier: VWR International
Description: VWR® Micro Star 21 ventilated and 21R refrigerated microcentrifuge with 24×1.5/2.0 ml rotor with ClickSeal™ biocontainment lid offer exceptional acceleration of up to 21000 xg in as little as 12 seconds.

Product Image-89259-890

VWR® Micro Spatulas, Double-Ended

Supplier: VWR International
Description: These VWR® Micro spatulas are double-ended and stainless steel.

Certificates

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