Plasma Membrane
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Starting at $89.00
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Starting at $89.00
Immunogen: AT2G24520 A0A1P8B2U9 
Synonyms: H+ATPase, AHA, ATHA, H(+)-ATPASE, HA, PLASMA MEMBRANE PROTON ATPASE, PMA Background:
Belongs to the P-type ATPase superfamily of cation-transporting ATPases, pumps protons out of the cell, generating a proton gradient that drives the active transport of nutrients by proton symport. has two autoinhibitory regions within the C-terminal domain. Its plasma membrane localization is light-dependent. -
Starting at $89.00
Immunogen: AT4G20260 Q96262 Synonyms: PCAP1, ARABIDOPSIS THALIANA PLASMA-MEMBRANE ASSOCIATED CATION-BINDING PROTEIN 1, ATPCAP1, MDP25, MICROTUBULE-DESTABILIZING PROTEIN 25, PLASMA-MEMBRANE ASSOCIATED CATION-BINDING PROTEIN 1 Background:
PCAP1 may be involved in intracellular signaling through interaction with PtdInsPs and calmodulin (CaM); it may keep PtdInsPs attached to the plasma membrane until Ca2+-CaM reaches a competitive concentration subsequent to an increase triggered by a stimulus, thus leading to PtdInsPs release and subsequent activation of InsPs-dependent signaling cascade. -
Starting at $89.00
Immunogen: AT2G17420 Q39242 Synonyms: Ntra, ATNTRA, NADPH-DEPENDENT THIOREDOXIN REDUCTASE 2, NADPH-DEPENDENT THIOREDOXIN REDUCTASE A, NTR2, THIOREDOXIN REDUCTASE A Background:
Thioredoxin (NTR/TRX) and glutathione (GSH/GRX) are the two major systems which play a key role in the maintenance of cellular redox homeostasis. They are essential for plant development, cell division or the response to environmental stresses. In Arabidopsis, three NTR proteins are including NTRA (AT2G17420), NTRB (AT4G35460), NTRC (AT2G41680). -
Starting at $89.00
Immunogen: AT2G16060 O24520 Synonyms: AHB1, ARATH GLB1, ATGLB1, CLASS I HEMOGLOBIN, GLB1, HB1, HEMOGLOBIN 1, NSHB1, PGB1, PHYTOGLOBIN 1 Background:
Different classes of nonsymbiotic plant hemoglobins have been identified and divided into class 1 (Hb1) and class 2 (Hb2) (AT3G10520) based on phylogenetic characteristics, gene expression patterns, and oxygen-binding properties. Type 1 nonsymbiotic hemoglobin from Arabidopsis thaliana (AHb1) shows a partial bis-histidyl hexacoordination but can reversibly bind diatomic ligands. AHB1 may not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule.
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