| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | CD44 antigen (CD44); partial; (CDw44)(Epican)(Extracellular matrix receptor III)(ECMR-III)(GP90 lymphocyte homing/adhesion receptor)(HUTCH-I)(Heparan sulfate proteoglycan)(Hermes antigen)(Hyaluronate receptor)(Phagocytic glycoprotein 1)(PGP-1)(Phagocytic glycoprotein I)(PGP-I)(CD antigen CD44) |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Reconstitution | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Overview
Recombinant Human CD44 antigen (CD44), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Immunology research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.
Key elements and design rationale
- Expressed region: 21-649aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
- Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
- Tag / fusion: N-terminal 6xHis-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
- Molecular weight (reported): 73.2 kDa. Apparent size may vary with tags, processing, and gel conditions.
When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.
Biological background
The gene commonly associated with this target is CD44. CD44 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.
Research relevance and current trends
- Profiling immune signaling nodes and cytokine pathways across cell types and activation states.
- Studying ligand–receptor interactions that shape immune cell communication and effector function.
- Building quantitative assays to compare pathway modulation by genetic or pharmacologic perturbations.
Relevance: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
Common research applications
- Assay and standard development for immunoassays or binding-based detection methods.
- Protein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.
- Structure–function analysis, including domain mapping or evaluation of sequence variants.
In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.
Notes for experimental interpretation
- Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
- Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
- Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
- E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
