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Agrisera
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Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
For reconstitution add 50 µL of sterile water.
Specific Species Reactivity: Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
CsoS1A, CsoS1B, and CsoS1C encode closely related bacterial microcompartment (BMC) domain shell proteins that localize to the facets of alpha-carboxysomes in chemoautotrophic bacteria, where they form the semi-permeable outer layer surrounding the carbon-fixation enzymes RuBisCO and carbonic anhydrase. Structurally, CsoS1 paralogs adopt a conserved alpha/beta BMC fold and oligomerize into cyclic hexamers that tile into extended, capsid-like molecular sheets; the hexamers are thin and characteristically asymmetric (one face more concave than the other) and contain a narrow central pore. These pores can bind anions and are thought to provide controlled diffusion routes across the shell, supporting selective metabolite flux (e.g., promoting passage of bicarbonate and other small anionic species) while helping maintain a microenvironment that enhances CO2 fixation efficiency by elevating CO2 availability near encapsulated RuBisCO. CsoS1A and CsoS1C are often highly similar and behave as interchangeable major facet components, whereas CsoS1B is typically a lower-abundance paralog that can form hexamers and may co-assemble with other CsoS1 subunits, contributing to shell architecture and permeability tuning during carboxysome assembly.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: csoS1; Hneap_0914; Hneap_0915; Hneap_0916