Plasma Membrane
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Starting at $89.00
Immunogen: AT2G45960 Q06611 
Synonyms: PIP1-2, ATHH2, NAMED PLASMA MEMBRANE INTRINSIC PROTEIN 1;2, PIP1;2, PIP1B, PLASMA MEMBRANE INTRINSIC PROTEIN 1B, TMP-A, TRANSMEMBRANE PROTEIN A Background:
PIPs proteins are aquaporins which selectively conduct water molecules in and out of the cell, while preventing the passage of ions and other solutes. PIPs are also known as water channels, aquaporins are integral membrane pore proteins. Some of them, known as aquaglyceroporins, also transport other small uncharged solutes, such as glycerol, CO2, ammonia and urea across the membrane, depending on the size of the pore. -
Starting at $89.00
Immunogen: AT3G61430 P61837 Synonyms: PIP1-1, ARABIDOPSIS THALIANA PLASMA MEMBRANE INTRINSIC PROTEIN 1, ATPIP1, PIP1, PIP1;1, PIP1A, PLASMA MEMBRANE INTRINSIC PROTEIN 1, PLASMA MEMBRANE INTRINSIC PROTEIN 1;1, PLASMA MEMBRANE INTRINSIC PROTEIN 1A Background:
PIPs proteins are aquaporins which selectively conduct water molecules in and out of the cell, while preventing the passage of ions and other solutes. PIPs are also known as water channels, aquaporins are integral membrane pore proteins. Some of them, known as aquaglyceroporins, also transport other small uncharged solutes, such as glycerol, CO2, ammonia and urea across the membrane, depending on the size of the pore. -
Starting at $89.00
Immunogen: AT5G27930 Q0WRB2 Synonyms: EGR2, E GROWTH-REGULATING 2 Background:
EGR2 is a negative regulator of plant growth with prominent effect on plant growth during drought stress. EGR2 regulates microtubule organization and likely affects additional cytoskeleton and trafficking processes along the plasma membrane. -
Starting at $89.00
Immunogen: AT2G33580 O22808 Synonyms: LYK5, ATLYK5, LYSM-CONTAINING RECEPTOR-LIKE KINASE 5 Background:
LYK5 is a putative LysM-containing receptor-like kinase. LYK5 is a major chitin receptor and forms a chitin-induced complex with related kinase CERK1. Based on protein sequence alignment analysis, it was determined as a pseudo kinase due to a lack of the ATP-binding P-loop in the kinase domain.
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