ActiveMax® Recombinant Human IL-7 Protein, premium grade, 50µg

Background
Interleukin 7 is also known as IL7, IL-7, and is a hematopoietic growth factor secreted by stromal cells in the red marrow and thymus. It is also produced by keratinocytes, dendritic cells, hepatocytes, neurons, and epithelial cells, but is not produced by lymphocytes. IL-7 stimulates the differentiation of multipotent (pluripotent) hematopoietic stem cells into lymphoid progenitor cells, It also stimulates proliferation of all cells in the lymphoid lineage (B cells, T cells and NK cells). It is important for proliferation during certain stages of B-cell maturation, T and NK cell survival, development and homeostasis. IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. IL-7 binds to the IL-7 receptor, a heterodimer consisting of Interleukin-7 receptor alpha and common gamma chain receptor. Il-7 promotes hematological malignacies (acute lymphoblastic leukemia, T cell lymphoma). Elevated levels of IL-7 have also been detected in the plasma of HIV-infected patients. IL-7 as an immunotherapy agent has been examined in many pre-clinical animal studies and more recently in human clinical trials for various malignancies and during HIV infection. IL-7 could also be beneficial in improving immune recovery after allogenic stem cell transplant.

Source
Recombinant Human IL-7, premium grade(IL7-H4219) is expressed from human 293 cells (HEK293). It contains AA Asp 26 - His 177 (Accession # P13232-1).
Predicted N-terminus: Asp 26
Human IL-7, premium grade (IL7-H4219), designed for preclinical stage, has the same activity and performance with GMP Human IL-7 (GMP-L07H24), which enables a seamless transition from preclinical development to clinical phases. Premium Grade product offer a cost efficient alternative of GMP Grade products for the early development phase when safety of raw materials is not top priority. By using Premium Grade products in early development phase, you can transition easily into clinical and commercial phase without need to revalidate the raw materials and modify manufacturing process.

Molecular Characterization
This protein carries no "tag".
The protein has a calculated MW of 17.4 kDa. The protein migrates as 23 kDa and 28 kDa (±3 kDa) when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin
Less than 0.01 EU per μg by the LAL method.

Host Cell Protein
<0.5 ng/ug of protein tested by ELISA.

Host Cell DNA
<0.02 ng/μg of protein tested by DNA fluorescent staining method.

Sterility
The sterility testing was performed by membrane filtration method.

Mycoplasma
Negative

Purity
>95% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

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.

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

Bioactivity
Please refer to product data sheet.

Clinical and Translational Updates

(1) "Identification and validation of immune-related genes in osteoarthritic synovial fibroblasts"
Dai, Chen, Zhang et al
Heliyon (2024) 10 (7), e28330
(2) "Understanding the pharmacokinetic journey of Fc-fusion protein, rhIL-7-hyFc using complementary approach of two analytical methods, accelerator mass spectrometry and ELISA"
Kim, Oh, Lee et al
Antib Ther (2024) 7 (2), 105-113
(3) "The Effects of Grape Seed Oligomeric Proanthocyanidin and Nisin on Dental Pulp Stem Cells"
Ballikaya, Babadag, San Keskin et al
Acta Stomatol Croat (2024) 58 (1), 2-17
Showing 1-3 of 7725 papers.