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Key Documents

SRP3189

Sigma-Aldrich

APRIL from mouse

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Sinónimos:

CD256, TALL-2, ZTNF2, A Proliferating-inducing Ligand, TNFSF13, TRDL-1a

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

mouse

recombinant

expressed in E. coli

assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

mol wt

21.9 kDa

packaging

pkg of 20 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white to off-white

Protein ID accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

mouse ... TNFSF13(69583)

General description

Research area: Immunology and Cytokines

APRIL (a proliferation-inducing ligand) was identified in 1998 through database mining and is a member of the TNF (tumor necrosis factor) family. APRIL gene is localized to human chromosome 17p13, contains six exons, and is alternatively transcribed to 1.8, 2.1, and 2.4 kb mRNA transcripts. APRIL protein is composed of a cytosolic domain of 28 amino acids, and a transmembrane region. It also contains an exoplasmic region, made up of a stalk and a TNF domain. It shares the highest similarity to BLyS (B lymphocyte stimulator) protein, ~30% sequence similarity in the TNF domain. It is synthesized as a type II transmembrane protein and is proteolytically processed as a mature protein, which is a soluble and non-covalent trimer. Recombinant murine APRIL is a soluble 21.9 kDa protein, consisting of 192 amino acid residues.

Biochem/physiol Actions

A proliferation-inducing ligand (APRIL) and its ligand interaction activate several signaling pathways, including nuclear factor-kappa B (NF-κB), p38, c-Jun N-terminal kinase mitogen-activated protein kinase (JNK MAPK), and Protein Kinase B/Forkhead Box O (AKT/FOXO), which are necessary for promoting the survival and differentiation of B cells and plasma cells. Additionally, APRIL signaling aids in the regulation of cytokine production, the generation of humoral immunity, decreases T cell-dependent antibody responses, and facilitates IgA class switching. These functions highlight the crucial role of APRIL in regulating immune responses. Furthermore, APRIL is also known to induce immune cell apoptosis leading to immunosuppression, and tumor development.

Sequence

MRREVSRLQR SGGPSQKQGE RPWQSLWEQS PDVLEAWKDG AKSRRRRAVL TQKHKKKHSV LHLVPVNITS KDSDVTEVMW QPVLRRGRGL EAQGDIVRVW DTGIYLLYSQ VLFHDVTFTM GQVVSREGQG RRETLFRCIR SMPSDPDRAY NSCYSAGVFH LHQGDIITVK IPRANAKLSL SPHGTFLGFV KL

Physical form

Lyophilized from 10 mM Sodium Acetate, pH 5.0 + 100 mM Arginine.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Visite la Librería de documentos

Tumor necrosis factor superfamily member APRIL contributes to fibrotic scar formation after spinal cord injury.
Funk LH. et al.
Journal of Neuroinflammation, 13(1) (2016)
TNFSF13 Is a Novel Onco-Inflammatory Marker and Correlates With Immune Infiltration in Gliomas
Chen R, et al.
Frontiers in immunology (2021)
APRIL Drives a Coordinated but Diverse Response as a Foundation for Plasma Cell Longevity
Stephenson S, et al.
Journal of Immunology, 209(5), 926-937 (2022)
Tarlan Mamedov et al.
PloS one, 14(3), e0213438-e0213438 (2019-03-13)
A plant expression platform with eukaryotic post-translational modification (PTM) machinery has many advantages compared to other protein expression systems. This promising technology is useful for the production of a variety of recombinant proteins including, therapeutic proteins, vaccine antigens, native additives
An APRIL to remember: novel TNF ligands as therapeutic targets.
Dillon SR, et al.
Nature Reviews. Drug Discovery, 5(3), 235-246 (2006)

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