Recombinant E. coli Glutamate/aspartate import solute-binding protein (Tagged) is a Escherichia coli K-12 Full Length protein, in the 23 to 302 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
No
D D A A P A A G S T L D K I A K N G V I V V G H R E S S V P F S Y Y D N Q Q K V V G Y S Q D Y S N A I V E A V K K K L N K P D L Q V K L I P I T S Q N R I P L L Q N G T F D F E C G S T T N N V E R Q K Q A A F S D T I F V V G T R L L T K K G G D I K D F A N L K D K A V V V T S G T T S E V L L N K L N E E Q K M N M R I I S A K D H G D S F R T L E S G R A V A F M M D D A L L A G E R A K A K K P D N W E I V G K P Q S Q E A Y G C M L R K D D P Q F K K L M D D T I A Q V Q T S G E A E K W F D K W F K N P I P P K N L N M N F E L S D E M K A L F K E P N D K A L N
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Binds to both glutamate and aspartate.
Glutamate/aspartate import solute-binding protein
Glutamate/aspartate import solute-binding protein, gltI, ybeJ, yzzK, b0655, JW5092
Recombinant E. coli Glutamate/aspartate import solute-binding protein (Tagged) is a Escherichia coli K-12 Full Length protein, in the 23 to 302 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE
No
No
Escherichia coli K-12
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
D D A A P A A G S T L D K I A K N G V I V V G H R E S S V P F S Y Y D N Q Q K V V G Y S Q D Y S N A I V E A V K K K L N K P D L Q V K L I P I T S Q N R I P L L Q N G T F D F E C G S T T N N V E R Q K Q A A F S D T I F V V G T R L L T K K G G D I K D F A N L K D K A V V V T S G T T S E V L L N K L N E E Q K M N M R I I S A K D H G D S F R T L E S G R A V A F M M D D A L L A G E R A K A K K P D N W E I V G K P Q S Q E A Y G C M L R K D D P Q F K K L M D D T I A Q V Q T S G E A E K W F D K W F K N P I P P K N L N M N F E L S D E M K A L F K E P N D K A L N
Full Length
47.2 kDa
23 to 302
Recombinant
His tag N-Terminus
Liquid
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Binds to both glutamate and aspartate.
Belongs to the bacterial solute-binding protein 3 family.
Blue Ice
-20°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
The glutamate/aspartate import solute-binding protein also known as GltI or GltS works mechanically by binding glutamate and aspartate to facilitate their import into bacterial cells through an ATP-binding cassette transporter system. This protein usually binds these amino acids with high affinity allowing efficient transport across the cell membrane. GltI has an estimated molecular mass of around 40 kDa and is expressed in certain bacteria including Escherichia coli where it forms an essential part of the nutrient uptake system.
This protein plays an important role in bacterial nitrogen metabolism by facilitating the uptake of glutamate and aspartate. GltI functions as part of a larger transport complex which includes other components such as permeases and ATPase. This transport complex works together to ensure that glutamate and aspartate are efficiently imported into the cell supporting important metabolic processes that rely on these amino acids as nitrogen sources.
Glutamate/aspartate import solute-binding protein participates in the nitrogen assimilation and amino acid biosynthesis pathways. Within these pathways the protein works alongside other transport proteins such as the dicarboxylate transport systems to maintain the cellular levels of important metabolites. By collaborating with proteins like the GltP transporter GltI contributes to amino acid availability which supports protein synthesis and other cellular functions that are vital for bacterial growth and survival.
Dysfunction in proteins similar to the glutamate/aspartate import solute-binding protein can contribute to metabolic imbalances. Although GltI itself does not directly relate to human diseases its study can provide insights into bacterial pathogenicity and resistance. Disruptions in the metabolic pathways where homologous proteins play a similar role in amino acid uptake can relate to bacterial infections. Investigation of GltI can help understand how bacteria thrive in hostile environments providing critical information for developing novel antibacterial strategies.
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