6942 Results for: "Sampler+Racks&pageNo=39&view=list"

Supplier: FRISTADS KANSAS

Tubular knit T-shirts made from 100% ring-spun cotton (single jersey). The grey melange shirt is made from 85% cotton and 15% viscose, while the yellow version is made from 65% polyester and 35% cotton.

Supplier: RENTEX

Work jacket made from blended fabric, 65% polyester and 35% cotton, pre-shrunk.

Supplier: Corning

PP translucent or PS clear, with PE screw cap. Straight walled vessels for sample collection, storage and transport. Twist closure for quick opening and closing, with leakproof inner lip. PS offers good thermal and chemical resistance. PP offers excellent thermal and chemical resistance.

Supplier: TRENKA

This exclusive fine piqué polo shirt is made from 100% ring-spun combed cotton. The gray model is made from 90% preshrunk ring-spun combed cotton and 10% viscose.

Supplier: RENTEX

Work jacket made from blended fabric, 65% polyester and 35% cotton, pre-shrunk.

Supplier: RENTEX

Bib and braces, Overall, bib and brace, Bib and braces, TrenkaTex®, 40 (men), Polyester/cotton, Beige, For men, 65% Polyester, 35% Cotton, Weight: 245 g/m², General Purpose, Pockets: With pockets

Supplier: FRISTADS KANSAS

Gilets made from 65% polyester and 35% cotton; napped inner.

Supplier: VWR Collection

Short thread ND9 vials manufactured from 1st hydrolytic class borosilicate glass with flat bottom. They can be purchased with a variety of polypropylene seal styles and septa materials.

Supplier: ProSci Inc.

RBM39 is an RNA binding protein and possible splicing factor. It is found in the nucleus, where it colocalizes with core spliceosomal proteins. Studies of a mouse protein with high sequence similarity to this protein suggest that this protein may act as a transcriptional coactivator for JUN/AP-1 and estrogen receptors.The protein encoded by this gene is an RNA binding protein and possible splicing factor. The encoded protein is found in the nucleus, where it colocalizes with core spliceosomal proteins. Studies of a mouse protein with high sequence similarity to this protein suggest that this protein may act as a transcriptional coactivator for JUN/AP-1 and estrogen receptors. Multiple transcript variants encoding different isoforms have been observed for this gene.

Supplier: COTTON CLASSICS HANDELS

Poloshirts, Poloshirts, Fruit of the Loom, L, Polyester/cotton, Grey, For men, 65% Polyester, 35% Baumwolle, Weight: 220/230 g/m², General Purpose, Pockets: Without pockets, Closure type: Buttons

Supplier: Portwest

These basic work trousers for men can be used as a part of a uniform, in service and office environments. They are made of 65% polyester and 35% cotton.

Supplier: NEW PIG

Formable socks hug corners and surround machine bases to absorb machine leaks, contain puddles and help keep workers safe.

Supplier: ProSci Inc.

ZIP6 Antibody: The zinc transporter ZIP6, also known as SLC39A6, is a member of a family of divalent ion transporters. Zinc is an essential ion for cells and plays significant roles in the growth, development, and differentiation. ZIP6 was initially identified as LIV-1, an estrogen-regulated gene that has been implicated in metastatic breast cancer. Elevated ZIP6 expression has also been reported in human cervical cancer and the HeLa cell line; down-regulation of ZIP6 expression in HeLa by RNAi inhibited cell proliferation, colony formation, migration and invasiveness, as well as decreasing Snail and Slug levels, suggesting ZIP6 plays a regulatory role on the ERK1/2-Snail/Slug pathway.

Supplier: ProSci Inc.

ZIP1 Antibody: ZIP1, also known as ZIRTL (zinc-iron regulated transporter-like), is the first mammalian member of a family of divalent ion transporters. Zinc is an essential ion for cells and plays significant roles in the growth, development, and differentiation. ZIP1 expression is markedly downregulated in a number of cancerous tissues and is thought to function as a tumor suppressor gene in prostate cancer. More recent studies have shown that overexpression of ZIP1 and concomitant increased levels of intracellular zinc in PC-3 cells cause a significant inhibition of NF-kappa B, leading to down-regulation of the antiapoptotic protein Bcl-2, Bcl-XL, and the apoptosis inhibitor XIAP, reducing the malignant potential of prostate cancer cells in vitro and in vivo.

Supplier: FRISTADS KANSAS

Overalls made from 65% polyester, 35% cotton, with soft nap on reverse side.

Supplier: SI Analytics

The Titroline® 7800 enhanced the universal features of the TitroLine® 7750 (potentiometric titration and volumetric KF titration), with an additional IDS measurement socket. Hence the TitroLine® 7800 is able to perform potentiometric titrations with analogue or IDS® electrodes as well as volumetric Karl Fischer titrations. The digital (IDS) measurement socket allows the connection of various digital sensors, such as for measuring of conductivity.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Sartorius Balances

Quintix® Pro laboratory balances are not just about meeting your expectations but exceeding them. The balances have an array of premium features that enhance usability, flexibility, and incorporate an eco-friendly design.

Supplier: Brady

Self-laminating vinyl (B-427) is an excellent material for wire and cable identification. This material has good clarity and conformability, and is self-extinguishing.

Supplier: ALSICO

Men's trousers with a modern, preshaped fitting that offers a professional look without compromising comfort. The fabric is powered by Alsiflex technology, which provides a unique combination of stretch, sustainability, and performance.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: ROBU GLASFILTER

VitraPOR® quartz glass filters offer exceptional thermal and chemical resistance for demanding filtration tasks. Ideal for high-temperature and aggressive environments, they ensure precise particle retention with excellent purity and mechanical strength.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.