Recombinant Full Length Photorhabdus Luminescens Subsp. Laumondii Undecaprenyl-Phosphate 4-Deoxy-4-Formamido-L-Arabinose Transferase(Arnc) Protein, His-Tagged
Cat.No. : | RFL22867PF |
Product Overview : | Recombinant Full Length Photorhabdus luminescens subsp. laumondii Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase(arnC) Protein (Q7N3Q6) (1-325aa), fused to N-terminal His tag, was expressed in E. coli. |
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Source : | E.coli expression system |
Species : | Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) |
Tag : | His |
Form : | Lyophilized powder |
Protein Length : | Full Length (1-325) |
AA Sequence : | MSFEQIKKVSVVIPIYNEEESLPLL LERTLAACKQLTQEYELILVDDGSS DKSAEILIQA AEQPENHIIAILLNRNYGQHSAIMA GFNQVNGDLIITLDADLQNPPEEIP RLVKTAEQGY DVVGTRRANRQDSLFRKTASKIINA MITKATGRSMGDYGCMLRAYRRHIV EAMLQCHERS TFIPILANTFARKTIEIDVAHAERE FGDSKYSFMKLINLMYDLLTCLTTA PLRLLSVVGS VIAVSGFLLAVLLMVLRLIFGAIWA AEGVFTLFALLFIFIGAQFVAMGLL GEYIGRIYND VRARPRYFIQKVVGDNKTNDNQEEY |
Purity : | Greater than 90% as determined by SDS-PAGE. |
Notes : | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Storage : | Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles. |
Storage Buffer : | Tris/PBS-based buffer, 6% Trehalose, pH 8.0 |
Reconstitution : | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
Gene Name : | arnC |
Synonyms : | arnC; pbgP; pmrF; plu2659; Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase; Polymyxin resistance protein PmrF; Undecaprenyl-phosphate Ara4FN transferase; Ara4FN transferase |
UniProt ID : | Q7N3Q6 |
Gene Name : | arnC |
Synonyms : | arnC; pbgP; pmrF; plu2659; Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase; Polymyxin resistance protein PmrF; Undecaprenyl-phosphate Ara4FN transferase; Ara4FN transferase |
UniProt ID : | Q7N3Q6 |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (21)
Ask a questionThe ArnC protein is primarily found in bacteria, more specifically in Gram-negative bacteria. It is not known to be present in other organisms such as eukaryotes or archaea.
Yes, mutations in the ArnC gene can confer resistance to certain antibiotics, particularly those that target the lipid A component of LPS. By modifying lipid A, the ArnC protein can modify the target site of antibiotics, reducing their effectiveness.
The ArnC protein and the LPS biosynthesis pathway it is involved in are potential targets for developing novel antimicrobial strategies. Inhibiting specific enzymes or disrupting LPS modifications could help enhance the effectiveness of existing antibiotics and combat antibiotic resistance.
Bacteria can develop resistance to ArnC-mediated LPS modifications through mutations in the ArnC gene itself or in other genes within the LPS biosynthesis pathway. These mutations can prevent or alter L-Ara4N addition to lipid A, reducing the effectiveness of the modification and potentially rendering bacteria more susceptible to certain antibiotics.
The ArnC protein belongs to the family of CoA-transferases and contains conserved functional domains such as the CoA-binding domain. These domains are essential for its enzymatic activity in transferring L-Ara4N to lipid A.
The ArnC protein is not universally conserved among all bacterial species. It is primarily found in Gram-negative bacteria, but its presence and occurrence can vary among different species.
The ArnC protein is found in multiple Gram-negative bacteria, including Escherichia coli, Salmonella enterica, and Klebsiella pneumoniae. However, its presence and exact function may vary among different bacterial species.
The ArnC protein can potentially be targeted with small molecules or inhibitors in drug development efforts related to combating bacterial infections. However, more research is needed to fully understand the structure and active sites of the protein in order to design specific inhibitors.
The ArnC protein itself is not commonly considered a vaccine target. However, its role in LPS modification and bacterial virulence makes it an important component to consider when designing vaccines targeting specific bacterial pathogens.
Currently, there are no known specific inhibitors or drugs that directly target the ArnC protein. However, research efforts are ongoing to develop inhibitors that can block or disrupt LPS modifications, including those involving ArnC, as a potential strategy to combat antibiotic resistance.
Natural variants or polymorphisms of the ArnC gene have not been extensively studied. However, sequence variations within the ArnC gene may occur among different bacterial strains, potentially affecting their susceptibility to antibiotics.
There is evidence of natural variation in the ArnC protein among different bacterial species. Due to horizontal gene transfer and genetic variation, different bacterial strains may have distinct versions of the ArnC protein, leading to variations in LPS modifications and potential differences in virulence and antibiotic resistance.
While the ArnC protein itself is not commonly used as a diagnostic marker, the detection of LPS modifications, including those involving L-Ara4N addition by ArnC, can provide valuable information for the diagnosis and treatment of certain bacterial infections.
Yes, the ArnC protein can contribute to bacterial virulence. Its ability to modify LPS can help bacteria evade host immune responses, promoting bacterial survival and establishment of infection.
Mutations or deletions in the ArnC gene can result in altered LPS composition and bacterial surface features. This can affect bacterial virulence, ability to interact with the host immune system, and susceptibility to certain antibiotics.
The ArnC protein affects the interaction of bacteria with their environment by modifying the LPS structure, which is crucial for bacterial adhesion, biofilm formation, and evasion of host immune responses. Changes in LPS composition due to ArnC-mediated modifications can alter these interactions and affect bacterial survival and colonization.
While the ArnC protein plays a crucial role in the modification of LPS, it is not considered essential for bacterial survival. Bacteria lacking functional ArnC can still survive but may exhibit altered LPS composition, which can affect their interactions with the host environment.
The expression of the ArnC gene is regulated by various regulatory mechanisms. It can be controlled by transcription factors, such as two-component systems or specific global regulators, which respond to environmental signals and control the expression of LPS biosynthesis genes.
The ArnC protein can contribute to antibiotic resistance by modifying the structure of the bacterial outer membrane through LPS modifications. These modifications can reduce the binding and effectiveness of certain antibiotics, making bacteria more resistant to their action.
The ArnC protein catalyzes the transfer of a 4-amino-4-deoxy-L-arabinose (L-Ara4N) molecule to lipid A, a component of LPS. This modification helps protect bacteria from the harmful effects of certain antibiotics and host immune responses.
Antimicrobial peptides produced by the host immune system can trigger the expression of the ArnC gene and subsequently the production of the ArnC protein. This helps bacteria modify their LPS and resist the antimicrobial effects of these peptides.
Customer Reviews (6)
Write a reviewWith its well-characterized nature and availability in various formats, the arnC protein is an advantageous tool that aids researchers in achieving their scientific goals.
the arnC protein is available in different formats, including recombinant and purified variants.
This flexibility allows researchers to select the most suitable form for their particular experimental setup, enhancing the efficiency and accuracy of their trials.
Its usage in these techniques is highly praised by scientists worldwide, attesting to its effectiveness and significance in advancing scientific knowledge and understanding.
Its ability to consistently provide accurate and reliable results makes it an invaluable tool for quantifying and detecting specific targets in biological samples.
The arnC protein's exceptional performance in ELISA and its successful application in protein electron microscopy structure analysis make it a highly reliable and recommended choice for researchers.
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