| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | High mobility group protein B1; High mobility group protein 1; HMG-1; HMGB1; HMG1 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of human Transferrin, different from the related mouse and rat sequences by five amino acids. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-Transferrin/TF Antibody Picoband® (monoclonal, 7I11B10) is an antibody reagent for detection of TF (high mobility group box 1). Researchers commonly use anti-TF antibodies to measure relative expression and localization across biological samples, with assay selection guided by the listed applications (WB, IHC, Flow, ELISA).
Boster Bio Anti-Transferrin/TF Antibody Picoband® (monoclonal, 7I11B10) catalog # M00094-5. Tested in WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Target: TF (high mobility group box 1). Alternative names: High mobility group protein B1; High mobility group protein 1; HMG-1; HMGB1; HMG1
- Antibody format: Monoclonal; clone 7I11B10; IgG2b
- Species context: Host: Mouse, Reactivity: Human,Mouse,Rat
- Purification: Immunogen affinity purified.
- Immunogen: A synthetic peptide corresponding to a sequence at the N-terminus of human Transferrin, different from the related mouse and rat sequences by five amino acids.
- Molecular weight context: observed 77 kDa (reported)
- Provided application(s): WB, IHC, Flow, ELISA
These attributes help contextualize how the antibody is commonly selected (host/clonality/isotype/label) and how signals are interpreted across sample types and assay formats.
Biological background
Function: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V (D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP.
Cellular localization: Nucleus. Endosome. Secreted. Cell membrane. Peripheral membrane protein. Extracellular side. Chromosome. Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment.
Tissue details: Ubiquituous. Expressed in platelets.
Background: Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. In humans, it is encoded by the TF gene. Transferrin consists of a polypeptide chain containing 679 amino acids in humans. The protein is composed of alpha helices and beta sheets to form two domains. The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. Transferrin is a glycoprotein that binds iron very tightly but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). And Transferrin has a molecular weight of around 80 kDa and contains 2 specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (1023 M1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.
Cross reactivity: No cross-reactivity with other proteins.
Research relevance and current trends
- Quantitative and spatial profiling: expression patterns are increasingly studied across cell states using multiplex imaging and omics-informed validation.
- Isoforms and post-translational modifications: researchers often evaluate how isoform composition and PTMs can shift apparent molecular weight or localization.
- Context-aware interpretation: comparative studies commonly include perturbations (stimulation, inhibition, genetic models) to relate target changes to pathway behavior.
Common research applications
- Western blot (WB): compare relative target abundance and apparent size shifts (e.g., isoforms/PTMs) across conditions.
- Immunohistochemistry (IHC): assess distribution across tissue compartments and compare staining patterns between groups.
- Flow cytometry: quantify target-positive populations and compare shifts after stimulation or differentiation.
Across these uses, researchers typically interpret changes in signal as relative differences between matched sample groups, considering sample preparation and biological context.
Notes for experimental interpretation
- Apparent molecular weight can vary due to isoforms, proteolysis, glycosylation, phosphorylation, and sample preparation differences.
- Species reactivity and epitope conservation can influence observed signal patterns, especially in cross-species studies.
- Control concepts: include appropriate negative controls (e.g., isotype controls where relevant) and, when feasible, genetic or orthogonal controls (KO/KD, peptide competition, or independent assays) to support interpretation.
For antibody reagents, monoclonal antibodies are often chosen for epitope consistency across lots, while polyclonals may recognize multiple epitopes and can show different background characteristics depending on context.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.