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Recombinant Protein L, His Tag

分子别名(Synonym)

RPL,Protein L

表达区间及表达系统(Source)

Recombinant Protein L, His Tag, also known as Recombinant Peptostreptococcus magnus Protein L, was expressed in E. coli at ACRObiosystems.

蛋白结构(Molecular Characterization)

Protein L Structure

Recombinant Protein L, His Tag is fused with the polyhistidine tag at N-terminus and a single cysteine at C-terminus. The reducing (R) protein migrates as a 45 kDa polypeptide when calibrated against Star Ribbon Pre-stained Protein Marker. Protein L Protein can bind to VL-Kappa.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>95% as determined by SDS-PAGE.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in 100 mM NaH2PO4, pH8.5 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

Protein L SDS-PAGE

Recombinant Protein L, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

 
评论(1)
  1. 416XXXXXXX63
  2. 3人赞
  3. I used recombinant protein L from ACROS Biosystems to prepare gold conjugates for immunosensors and rapid quantification of human IgG and was able to detect 2.5 ng of Human IgG in less than 1 minute. I highly recommend this product for the detection and isolation of antibodies and Fab'2 fragments. I will definitely be ordering this item again.
  4. 2021-10-3
 
ACRO质量管理体系
 
 

背景(Background)

Protein L was isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind Ig(IgG,IgM,IgA,IgE and IgD) through L chain interaction, from which the name was suggested. Despite this wide-ranging binding capability with respect to Ig classes, Protein L is not a universal immunoglobilin-binding protein. Binding of Protein L to immunoglobulins is restricted to those containing kappa light chains (i.e., k chain of the VL domain). In humans and mice, kappa (k) light chains predominate. The remaining immunoglobulins have lambda (l) light chains. The recombinant protein contains four immunoglobulin (Ig) binding domains (Bdomains) of the native protein. Besides antibody, protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs).

文献引用(Citations)

 

前沿进展

Genetic and transcriptomic analysis of lentil seed imbibition and dormancy in relation to its domestication
Guerra-García, Balarynová, Smykal et al
Plant Genome (2025) 18 (2), e70021
Abstract: Seed dormancy is an adaptation that delays germination to prevent the start of this process during unsuitable conditions. It is crucial in wild species but its loss was selected during crop domestication to ensure a fast and uniform germination. Water uptake, or imbibition, is the first step of germination. In the Fabaceae family, seeds have physical dormancy, in which seed coats are impermeable to water. We used an interspecific cross between an elite lentil line (Lens culinaris) and a wild lentil (L. orientalis) to investigate the genetic basis of imbibition capacity through quantitative trait locus (QTL) mapping and by using RNA from embryos and seed coats at different development stages, and phenotypic data of seed coat thickness (SCT) and proportion of imbibed seeds (PIS). Both characteristics were consistent throughout different years and locations, suggesting a hereditary component. QTL results suggest that they are each controlled by relatively few loci. Differentially expressed genes (DEGs) within the QTL were considered candidate genes. Two glycosyl-hydrolase genes (a β-glucosidase and a β-galactosidase), which degrade complex polysaccharides in the cell wall, were found among the candidate genes, and one of them had a positive correlation (β-glucosidase) between gene expression and imbibition capacity, and the other gene (β-galactosidase) presented a negative correlation between gene expression and SCT.© 2025 The Author(s). The Plant Genome published by Wiley Periodicals LLC on behalf of Crop Science Society of America.
Lethal and sublethal toxicity of ytterbium in rainbow trout juveniles
Auclair, Roubeau-Dumont, André et al
Environ Sci Pollut Res Int (2025)
Abstract: The heavy rare earth element ytterbium (Yb) is a critical element of technology finding its way into urban wastewaters from solid waste disposal sites. The purpose of this study was to investigate the lethal and sublethal toxicity of Yb to rainbow trout juveniles. They were exposed to increasing concentrations of Yb3+ (0.06-40 mg/L) for 96 h at 15 °C. Mortality was recorded, and in the surviving fish, the following biomarkers were determined: protein aggregation, thioneins, lipid peroxidation (LPO), and DNA damage in gills and the liver. The 96-h lethal concentration (LC50) was 2.7 ± 0.66 mg/L indicating that this element is toxic to fish. Biomarker responses to Yb occurred at concentration 45 times less than the LC50 in some cases. The following biomarkers were positively (p < 0.05) correlated to fish survival: liver thioneins, gill DNA strand breaks, LPO, and protein aggregation in the liver. The decrease in LPO in the liver and gills by Yb suggests reduced production of reactive oxygen species production. In conclusion, Yb is toxic to trout juveniles producing sublethal effects at concentrations range of 60 µg/L after 96 h. This concentration represents an upper limit for consideration for aquatic animal health.© 2025. Crown.
Effect of lipid-based nutrient supplements on morbidity among children with stunting: secondary analysis of a randomized trial in Uganda
Mutumba, Mbabazi, Pesu et al
Eur J Clin Nutr (2025)
Abstract: Children with stunting are at risk of infections. We assessed the effect of lipid-based nutrient supplement (LNS) on morbidity in children with stunting.This was a secondary analysis of a randomized, 2×2 factorial trial among 12-59 months-old, stunted children in Uganda. Children were randomized to LNS containing milk or soy protein and whey permeate or maltodextrin, or no supplementation, for 12 weeks. The outcomes were caregiver-reported morbidity after 2, 4, 8 and 12 weeks, serum C-reactive protein (S-CRP), α1-acid glycoprotein (S-AGP), and phase-angle (PhA) by bioimpedance.Of 750 children, mean (SD) age was 32.0 (11.7) months, 55% (n = 412) were male. LNS increased diarrhoea prevalence (18.1% vs 7.3%, P = 0.001) during the first two weeks, but not thereafter. There was no effect of LNS on cough or fever. LNS resulted in greater decline in S-AGP (-0.10 g/L, 95% CI: -0.17, -0.03, P = 0.003) but not S-CRP (25%, 95% CI: -11, 74, P = 0.193), and greater increase in PhA (0.10 degrees, 95% CI: 0.01, 0.18, P = 0.030), explained by greater fat-free mass. Milk compared to soy protein in LNS resulted in higher PhA (0.10 degrees, 95% CI: 0.02, 0.17, P = 0.013), not explained by fat-free mass.LNS supplementation in children with stunting had no effect on morbidity but resulted in a small reduction in sub-acute systemic inflammation. The possible effect of LNS supplementation on inflammation in stunted children requires further evaluation. ( www.isrctn.com : ISRCTN13093195).© 2025. The Author(s).
Circular RNA aptamers targeting neuroinflammation ameliorate Alzheimer disease phenotypes in mouse models
Feng, Jiang, Zhai et al
Nat Biotechnol (2025)
Abstract: Alzheimer disease (AD) therapy may benefit from optimized approaches to inhibit neuroinflammation. Small-molecule inhibitors of the proinflammatory molecule double-stranded RNA (dsRNA)-activated protein kinase R (PKR) have efficacy in AD models but their utility is compromised by adverse side effects. Here, we target PKR in two mouse models of AD using circular RNAs containing short double-stranded regions (ds-cRNAs), which are structurally similar to what we used previously to target PKR in psoriasis models. We show that the intrahippocampal injection of ds-cRNAs to neurons and microglia by adeno-associated virus (AAV) effectively dampens excessive PKR activity with minimal toxicity, accompanied by reduced neuroinflammation and amyloid-β plaques. We also deliver ds-cRNAs to the whole brain through intravenous injection of AAV-PHP.eB, which crosses the blood-brain barrier, resulting in neuroprotection and enhanced capability of spatial learning and memory in AD mouse models. The delivery of ds-cRNAs at different progressive stages of AD alleviates disease phenotypes, with therapeutic effects sustained for at least 6 months after a single administration.© 2025. The Author(s), under exclusive licence to Springer Nature America, Inc.
Showing 1-4 of 642361 papers.
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