Supplier:
PORTWEST LLC.
Description:
Coveralls are designed to protect against radiant, convective, and contact heat.
Supplier:
AMBEED, INC
Description:
Methyl 5,5-difluoropiperidine-3-carboxylate, N-BOC protected 98%, Ambeed.Inc
Supplier:
Thermo Scientific Chemicals
Description:
Fieser: 9,54 13,241 14,257 15,257 16,274 18,289 19,41 20,305 21,342
Supplier:
Dickies
Description:
Dickies® style LP337.
Supplier:
AMBEED, INC
Description:
1,3-Bis(4-chlorophenyl)urea 98%
Supplier:
VWR
Description:
Substrate for the detection of horseradish peroxidase commonly used in ELISA. Read at 450 nm.
Supplier:
Thermo Scientific Chemicals
Description:
MDL: MFCD00008269
Beilstein Registry No.: 3607620
Supplier:
AMBEED, INC
Description:
4-Bromo-1,2-bis(trifluoromethyl)benzene, Purity: 97%, CAS Number: 320-29-6, Appearance: Liquid, Storage: Sealed in dry, Room Temperature, Size: 250mg
Supplier:
AMBEED, INC
Description:
Bis(pinacolato)diboron 98%
Supplier:
Strem Chemicals Inc
Description:
Phosphine
Supplier:
Strem Chemicals Inc
Description:
Metallocenes, Derivatives & Cp Precursors
Supplier:
AMBEED, INC
Description:
Bis(NHS)PEG₉ 98%
Catalog Number:
(10473-828)
Supplier:
Bioss
Description:
Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.
Catalog Number:
(10473-826)
Supplier:
Bioss
Description:
Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.
Catalog Number:
(10473-824)
Supplier:
Bioss
Description:
Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.
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