Analytical Data
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Gene name
ALF
- Application
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Alternative Names
GTF2A1L; ALF; GTF2A1LF; TFIIA-alpha and beta-like factor; General transcription factor II A; 1-like factor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UNN4
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Expression Region
251-348aa
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AA Sequence
PQVSQTNSNVESVLSGSASMAQNLHDESLSTSPHGALHQHVTDIQLHILK NRMYGCDSVKQPRNIEEPSNIPVSEKDSNSQVDLSIRVTDDDIGEIIQ
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Molecular Weight
52.4 KDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ALF (antimicrobial peptide from the Annelida family) recombinant proteins have garnered significant attention in recent years due to their potential applications in biotechnology and medicine. These proteins, derived from annelids, possess unique antimicrobial properties that make them promising candidates for the development of novel antibiotics, especially in the face of rising antibiotic resistance. The increasing prevalence of multidrug-resistant bacterial infections has led to an urgent need for new therapeutic options, and ALF proteins, with their ability to disrupt bacterial membranes and inhibit pathogen growth, may provide innovative solutions. Research has focused on understanding the structure-function relationship of these peptides, enabling the design of optimized variants with enhanced efficacy and stability. Advances in recombinant DNA technology have facilitated the production of ALF proteins in heterologous expression systems, allowing for large-scale production and detailed functional studies. Additionally, exploring the mechanism of action and potential synergistic effects with existing antibiotics could lead to the development of combination therapies that enhance treatment efficacy. Overall, the study of ALF recombinant proteins represents a promising frontier in the search for alternatives to conventional antibiotics, with the potential to address significant public health challenges posed by resistant pathogens.
