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 >  Protein>CD19 >CD9-H52H2

Human CD19 (20-291) Protein, His Tag (SPR verified) DMF

分子别名(Synonym)

CD19,B4,CVID3,MGC12802

表达区间及表达系统(Source)

Human CD19 (20-291), His Tag (CD9-H52H2) is expressed from human 293 cells (HEK293). It contains AA Pro 20 - Lys 291 (Accession # P15391-1).

Predicted N-terminus: Pro 20

Request for sequence

蛋白结构(Molecular Characterization)

CD19 Structure

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 32.0 kDa. The protein migrates as 43 kDa and 45-55 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>90% as determined by SDS-PAGE.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 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 6 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)

CD19 SDS-PAGE

Human CD19 (20-291), His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

 

活性(Bioactivity)-ELISA

CD19 ELISA

Immobilized Human CD19 (20-291), His Tag (Cat. No. CD9-H52H2) at 2 μg/mL (100 μL/well) can bind Monoclonal Anti-Human CD19 Antibody, Mouse IgG2a with a linear range of 0.2-3 ng/mL (QC tested).

Protocol

CD19 ELISA

Immobilized Human CD19 (20-291), His Tag (Cat. No. CD9-H52H2) at 2 μg/mL (100 μL/well) can bind different Anti-CD19 antibodies with high affinity (Routinely tested).

Protocol

 

活性(Bioactivity)-SPR

CD19 SPR

FMC63 MAb (Mouse lgG2a) captured on CM5 chip via anti-mouse antibodies surface can bind Human CD19 (20-291), His Tag (Cat. No. CD9-H52H2) with an affinity constant of 2.9 nM as determined in a SPR assay (Biacore 8K) (QC tested).

Protocol

 

活性(Bioactivity)-BLI

CD19 BLI

Loaded Monoclonal Anti-Human CD19 Antibody, Mouse IgG2a on AMC Biosensor, can bind Human CD19 (20-291), His Tag (Cat. No. CD9-H52H2) with an affinity constant of 3.19 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

Protocol

CD19 BLI

Loaded Monoclonal Anti-Human CD19 Antibody, Human IgG1 on AHC Biosensor, can bind Human CD19 (20-291), His Tag (Cat. No. CD9-H52H2) with an affinity constant of 4.28 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

Protocol

 

活性(Bioactivity)-FACS

CD19 FACS

2e5 of anti-CD19 CAR-293 cells were stained with 100 μL of 10 μg/mL of Human CD19 (20-291), His Tag (Cat. No. CD9-H52H2) and negative control protein respectively, washed and then followed by FITC anti-His tag antibody and analyzed with FACS (Routinely tested).

Protocol

 
 
ACRO质量管理体系
 
 

背景(Background)

B-lymphocyte antigen CD19 is also known as CD19 (Cluster of Differentiation 19), is a single-pass type I  membrane protein which contains two Ig-like C2-type (immunoglobulin-like) domains. CD19 is expressed on follicular dendritic cells and B cells. In fact, it is present on B cells from earliest recognizable B-lineage cells during development to B-cell blasts but is lost on maturation to plasma cells. It primarily acts as a B cell co-receptor in conjunction with CD21 and CD81. Upon activation, the cytoplasmic tail of CD19 becomes phosphorylated, which leads to binding by Src-family kinases and recruitment of PI-3 kinase. As on T cells, several surface molecules form the antigen receptor and form a complex on B lymphocytes. The (almost) B cell-specific CD19 phosphoglycoprotein is one of these molecules. The others are CD21 and CD81. These surface immunoglobulin (sIg)-associated molecules facilitate signal transduction. On living B cells, anti-immunoglobulin antibody mimicking exogenous antigen causes CD19 to bind to sIg and internalize with it. The reverse process has not been demonstrated, suggesting that formation of this receptor complex is antigen-induced. This molecular association has been confirmed by chemical studies. Mutations in CD19 are associated with severe immunodeficiency syndromes characterized by diminished antibody production. CD19 has been shown to interact with: CD81, CD82, Complement receptor 2, and VAV2.

文献引用(Citations)

 

前沿进展

Follicle-Stimulating Hormone and Testosterone Play a Role in the Regulation of Sertoli Cell Functions Following Germ Cell Depletion In Vitro
Sawaied, Levy, Arazi et al
Int J Mol Sci (2025) 26 (6)
Abstract: Spermatogenesis is a process of self-renewal of spermatogonial stem cells and their proliferation and differentiation to generate mature sperm. This process involves interactions between testicular somatic (mainly Sertoli cells) and spermatogonial cells at their different stages of development. The functionality of Sertoli cells is regulated by hormones and testicular autocrine/paracrine factors. In this study, we investigated the effects of follicle-stimulating hormone (FSH) and testosterone addition on Sertoli cell cultures that undergo hypotonic shock, with a primary focus on Sertoli cell activity. Cells were enzymatically isolated from testicular seminiferous tubules of 7-day-old mice. These cells were cultured in vitro for 3 days. Thereafter, some cultures were treated with hypotonic shock to remove germ cells. After overnight, fresh media without (control; CT) or with FSH, testosterone (Tes), or FSH+T were added to the hypotonic shock-treated or untreated (CT) cultures for 24 h. The morphology of the cultures and the presence of Sertoli cells and germ cells were examined. The expression of growth factors (CSF-1, LIF, SCF, GDNF) or other specific Sertoli cell factors [transferrin, inhibin b, androgen receptor (AR), androgen binding protein (ABP), FSH receptor (FSHR)] was examined by qPCR. Our immunofluorescence staining showed depletion/major reduction in VASA-positive germ cells in Sertoli cell cultures following hypotonic shock (HYP) treatment compared to untreated cultures (WO). Furthermore, the expression of the examined growth factors and other factors was significantly increased in HYP cultures compared to WO (in the CT). However, the addition of hormones significantly decreased the expression levels of the growth factors in HYP cultures compared to WO cultures under the same treatment. In addition, the expression of all other examined Sertoli cell factors significantly changed following HYP treatment compared to WO and following treatment with FSH and or T. However, the expression levels of some factors remained normal following the treatment of Sertoli cell cultures with one or both hormones (transferrin, Fsh-r, Abp, Ar). Thus, our results demonstrate the crucial role of germ cells in the functionality of Sertoli cells and the possible role of FSH and T in maintaining, at least partially, the normal activity of Sertoli cells following germ cell depletion in vitro by hypotonic shock treatment.
Taming Lithium Nucleation and Growth on Cu Current Collector by Electrochemical Activation of ZnF2 Layer
Nguyen, Shim, Byeon et al
Adv Sci (Weinh) (2025)
Abstract: Lithium-metal anodes are essential for the advancement of next-generation batteries. However, their practical use is largely hindered by the uncontrollable growth of dendrites and intricate problems associated with fabricating anodes that meet capacity requirements. Here, it is demonstrated that an ultrathin ZnF2 layer deposited on the copper foil can produce a novel and efficient current collector to address these challenges. It is observed that ZnF2 can be transformed into LiZn alloy and LiF salt in one step by simple electrochemical activation. The resulting LiZn alloy exhibits high lithiophilicity, which reduces overpotential and promotes uniform lithium nucleation, while the LiF salt enhances the solid electrolyte interphase, ensuring uniform lithium growth. This synergistic effect led to a dendrite-free, densely packed lithium anode with an extended lifespan, achieving over 900 h in symmetric cells at a high current density of 3 mA cm-2 and a high cut-off capacity of 3 mAh cm-2. Furthermore, full cells utilizing the lithium anode (Li capacity of 6 mAh cm-2) paired with LiNi0.8Mn0.1Co0.1O2 cathodes (mass loading of 11.5 mg cm-2) demonstrates drastically improved rate capability and excellent cycling stability. This approach holds great promise for developing safer and more efficient lithium-metal-based batteries for future energy storage solutions.© 2025 The Author(s). Advanced Science published by Wiley‐VCH GmbH.
Eco-friendly extraction of hesperidin from citrus peels: a comparative study of Soxhlet, ultrasound-assisted, and microwave-assisted methods for improved yield and antioxidant properties
Yeddes, Bettaieb Rebey, Yazidi et al
Int J Environ Health Res (2025)
Abstract: This study compares Soxhlet extraction, ultrasound-assisted extraction (UAE), and microwave-assisted extraction (MAE) for isolating hesperidin from citrus peels. UAE achieved the highest yield (89.7%) and demonstrated favorable kinetic parameters (rate constant: 0.96 h-1, half-life: 0.72 h), highlighting its efficiency as an eco-friendly alternative. The UAE extract also exhibited the highest total phenolic and flavonoid contents, maximizing bioactive compound recovery. While MAE showed superior antioxidant activity in DPPH (IC₅₀: 31.49 µg/mg DE) and ABTS (IC₅₀: 73.38 µg/mg DE) assays, the HPLC analysis confirmed a hesperidin purity of 89.7%, with UAE and MAE yielding comparable results. These findings underscore UAE's potential for enhancing hesperidin extraction while promoting sustainability through citrus waste valorization. This research provides valuable insights into optimizing extraction techniques for bioactive compounds and supporting their industrial applications.
Peroxisome proliferator-activated receptor beta/delta ligands as modulators of immune response in lipopolysaccharide-stimulated porcine endometrium: insights from an in vitro study
Golubska, Bogacka, Mierzejewski et al
J Physiol Pharmacol (2025) 76 (1)
Abstract: Inflammation in the reproductive organs is a serious threat to human and animal fertility. Recently, the possible role of peroxisome proliferator-activated receptor (PPAR) ligands as potential regulators of endometrial inflammation has been proposed. The aim of the present study was to investigate the effect of PPARβ/δ ligands on mRNA abundance and protein secretion of selected inflammatory mediators - interleukin (IL)-1β, IL-6, IL-8, IL-4, IL-10, tumor necrosis factor alpha (TNF-α), leukemia inhibitory factor (LIF), toll-like receptor 4 (TLR4) and nuclear factor kappaB (NF-κB) - in porcine endometrium during physiology and lipopolysaccharide (LPS)-stimulated inflammation in both the mid-luteal and follicular phases of the estrous cycle. In addition, two experimental setups - an ongoing and a developing inflammation - were considered. Sections of endometrial tissue were incubated in vitro with two selected PPARβ/δ ligands: agonist L-165,041 or antagonist GSK 3787 with or without LPS. The mRNA abundance was determined by real time polymerase chain reaction (RT-PCR) and protein secretion in the culture medium by enzyme-linked immunosorbent assay (ELISA). Both PPARβ/δ ligands increased the mRNA abundance of IL-1β, IL-6 and IL-8 in the inflammatory state and decreased IL-4 protein secretion in the physiological state, mainly in the mid-luteal phase of the estrous cycle. In turn, only the antagonist increased TNF-α expression. For all proinflammatory cytokines - IL-1β, IL-6, IL-8, TNF-α - we found that both hormonal and inflammatory status significantly influenced their mRNA levels, while the experimental setup notably affected the expression of IL-1β, IL-6 and TNF-α. The results show that PPARβ/δ ligands modulate the expression and secretion of cytokines involved in the inflammatory response in the porcine endometrium. The main effect of PPARβ/δ ligands was noted during the mid-luteal phase of the estrous cycle. During LPS-stimulated inflammation, PPARβ/δ ligands appear to have pro-inflammatory properties by stimulating the expression of IL-1β, IL-6, IL-8, TNF-α. The changes in the expression of immune mediators depend on the phase of the estrous cycle or the course of endometritis.
Showing 1-4 of 12897 papers.
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CD19靶点信息
英文全称:B-lymphocyte antigen CD19
中文全称:B淋巴细胞抗原CD19
种类:Homo sapiens
上市药物数量:12详情
临床药物数量:310详情
最高研发阶段:申请上市
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