slc30a7 Antibody

What are the recommended applications for SLC30A7/ZnT7 antibodies?

SLC30A7 antibodies have been validated for multiple experimental applications:

Most commercial antibodies have undergone rigorous validation procedures. For example, Boster Bio reports validating all antibodies on WB, IHC, ICC, IF, and ELISA with known positive control and negative samples to ensure specificity and high affinity . Immunocytochemistry/immunofluorescence applications have demonstrated SLC30A7 localization to the Golgi apparatus in human A-431 cells , consistent with its biological function.

What are the optimal dilutions for different applications of SLC30A7 antibodies?

Based on multiple commercial sources, recommended dilutions vary by application:

These dilutions should be considered starting points. As stated in the Proteintech documentation: "It is recommended that this reagent should be titrated in each testing system to obtain optimal results" and results may be "sample-dependent" .

What positive controls are recommended for validating SLC30A7 antibody performance?

Researchers should consider the following validated positive controls:

• Western blot: C2C12 cells have demonstrated reliable detection

• IHC: Human lung cancer tissue shows positive staining , and human small intestine exhibits strong positivity in the luminal membrane of glandular cells

• IF/ICC: A431 cells show distinct Golgi apparatus localization

When establishing a new experimental system, running these controls alongside experimental samples provides confidence in antibody performance.

How can SLC30A7 antibodies be utilized to study zinc homeostasis dysregulation in disease models?

SLC30A7 plays critical roles in zinc homeostasis with implications for multiple diseases. When designing experiments:

• Cancer studies: Consider the upregulation pattern observed in cervical carcinoma. Recent research demonstrated that expression of SLC30A1, SLC30A7, and SLC30A10 was significantly higher in cervical carcinoma compared to normal matched tissues . The standard methodological approach involved:

  • IHC staining using rabbit polyclonal anti-SLC30A7 antibody (1:200 dilution)

  • Assessment using Remmele's semi-quantitative immune response score (IRS) scale

  • Classification of expression: <5 as low expression, ≥5 as high expression

• Diabetes/metabolic studies: Deletion of SLC30A7 impairs glucose tolerance and reduces the glucose-stimulated increase in plasma insulin levels, hepatic glycogen levels, and pancreatic insulin content . When using antibodies to study this system:

  • Compare isolated islets using free zinc detection assays alongside antibody detection

  • Consider the functional relationship with SLC30A8, as combined deletion of SLC30A7 and SLC30A8 abolishes glucose-stimulated insulin secretion

• Novel research direction: Recent findings suggest SLC30A7 involvement in cuproptosis regulation in glioblastoma multiforme via the JAK2/STAT3/ATP7A pathway . This represents an emerging area where antibody-based co-localization studies could prove valuable.

What methodological considerations are essential when investigating SLC30A7 subcellular localization?

When investigating SLC30A7 subcellular localization:

• Fixation protocol optimization: For immunofluorescence, use PFA/Triton X-100 fixation/permeabilization as recommended for SLC30A7 detection .

• Co-localization markers: Include antibodies against established Golgi markers, as SLC30A7 predominantly localizes to the Golgi apparatus.

• Antigen retrieval considerations:

  • For IHC paraffin sections, HIER pH 6 retrieval is recommended

  • Some protocols suggest TE buffer pH 9.0 for optimal results, with an alternative option of citrate buffer pH 6.0

• Resolution requirements: Use confocal microscopy with appropriate z-stack acquisition to accurately determine subcellular compartmentalization.

• Controls: Include known subcellular markers alongside SLC30A7 staining to validate localization patterns.

How can researchers interpret SLC30A7 and SLC30A8 co-expression data in metabolic disease models?

The functional relationship between SLC30A7 and SLC30A8 has significant implications for glucose metabolism and diabetes research. When studying their co-expression:

• Expression pattern analysis: Evidence suggests that deletion of SLC30A7 alone has complex effects in vivo but no effect on glucose-stimulated insulin secretion (GSIS) in isolated islets, whereas combined deletion of SLC30A7 and SLC30A8 abolishes GSIS .

• Interpretational framework:

  • Single protein expression changes may not predict functional outcomes due to compensatory mechanisms

  • Reduced SLC30A7 expression might induce compensatory changes in SLC30A8 activity

  • The function of ZnT8 (SLC30A8) in islets can be unmasked by removal of ZnT7 (SLC30A7)

• Methodological approach:

  • Use antibodies against both transporters in parallel samples

  • Quantify relative expression using standardized Western blot protocols

  • Consider genetic models (knockout/knockdown) alongside antibody-based detection to establish causal relationships

What are the most common technical challenges when using SLC30A7 antibodies and how can they be addressed?

Several technical issues may arise when working with SLC30A7 antibodies:

• Variable molecular weight detection:

  • Expected molecular weight: 42 kDa (as reported by Proteintech and Boster Bio )

  • Alternative observation: 65 kDa (as reported by FineTest )

  • Solution: Run appropriate positive controls to establish baseline detection pattern for your experimental system

• Antibody recycling concerns:

  • It is generally not recommended to recycle antibodies as buffer systems change after use

  • If necessary due to resource constraints, high titer antibodies may potentially be stored at 4°C for approximately one week and reused about three times

  • Performance efficiency of recycled antibodies cannot be guaranteed

• Storage considerations:

  • Store at -20°C for long-term storage

  • Avoid repeated freeze-thaw cycles

  • Most antibodies are stable for one year after shipment when properly stored

How can researchers optimize SLC30A7 antibody protocols for studying tissues with low expression levels?

When studying tissues with low SLC30A7 expression:

• Signal amplification strategies:

  • Consider tyramide signal amplification (TSA) for immunohistochemistry

  • Use higher antibody concentrations (within the upper range of manufacturer recommendations)

  • Extend primary antibody incubation time (overnight at 4°C)

• Detection system optimization:

  • For Western blot: Use high-sensitivity ECL substrates

  • For IHC/IF: Implement biotin-streptavidin amplification systems

  • Consider more sensitive detection methods like proximity ligation assay (PLA) for protein-protein interaction studies

• Sample preparation considerations:

  • Enrich for relevant subcellular fractions (e.g., Golgi isolation) before detection

  • Implement epitope retrieval optimization for tissue sections

What controls should be included when studying SLC30A7 in genetic manipulation models?

When studying SLC30A7 in knockout, knockdown, or overexpression models:

• Essential controls for knockout studies:

  • Wildtype samples processed identically to knockout samples

  • Heterozygous samples (if available) to assess gene dosage effects

  • Multiple antibodies targeting different epitopes to confirm specificity

• Validation approaches for knockdown experiments:

  • Scrambled shRNA controls processed in parallel

  • Concentration gradient of knockdown to assess antibody sensitivity

  • Complementary mRNA quantification to correlate with protein reduction

• Overexpression verification:

  • Empty vector controls

  • Tagged protein detection (if applicable) to verify expression alongside antibody detection

  • Functional assays to confirm biological activity of overexpressed protein

How can SLC30A7 antibodies be used to investigate the role of zinc transporters in cancer progression?

Recent research highlights potential roles for SLC30A7 in cancer biology:

• Cervical carcinoma applications:

  • SLC30A7 expression is significantly higher in cervical carcinoma than in normal matched tissues

  • Expression correlates with tumor stage (SLC30A7 groups significantly varied by stage)

  • Methodological approach: Use IHC scoring system with rabbit polyclonal anti-SLC30A7 antibody (1:200 dilution)

• Immune cell infiltration correlation:

  • Evidence suggests SLC30A family members may have regulatory roles in immune infiltration

  • For example, SLC30A1 showed moderate correlations with tumor-infiltrating lymphocytes including activated CD8 T cells and other immune cell populations

  • Experimental approach: Combine SLC30A7 antibody staining with immune cell markers in multiplexed immunofluorescence

• Therapeutic target investigation:

  • Novel research suggests SLC30A7 involvement in glioblastoma multiforme tumorigenicity via the JAK2/STAT3/ATP7A pathway

  • Experimental design should include co-staining with pathway components (p-JAK2, p-STAT3, ATP7A)

What methodological approaches are recommended for investigating SLC30A7 in rare genetic disorders?

Recent identification of SLC30A7 variants in human disease provides new research directions:

• Clinical phenotype correlation:

  • Compound heterozygous variants in SLC30A7 have been associated with stunted growth, testicular hypoplasia, and bone marrow failure in humans

  • Methodological approach: Combine genetic analysis with antibody-based protein quantification

• Variant impact assessment:

  • In documented cases, SLC30A7 protein expression was reduced by 80-96% in affected individuals compared to control cells

  • Recommended approach:

    • Use Western blot quantification with standardized loading controls

    • Compare with mRNA quantification to determine if reduction is transcriptional or post-transcriptional

• Functional studies in patient-derived cells:

  • Analysis of zinc transport activity alongside protein expression

  • Co-immunoprecipitation studies to assess potential altered protein interactions

How can researchers effectively combine SLC30A7 antibody detection with functional zinc transport assays?

To correlate SLC30A7 protein expression with functional zinc transport:

• Integrated experimental design:

  • Use antibody detection to quantify protein levels in parallel with zinc transport assays

  • In knockout studies, zinc content can be measured using assays that detect free or loosely bound zinc

• Subcellular zinc distribution analysis:

  • Combine SLC30A7 immunofluorescence with zinc-specific fluorescent probes

  • Correlate SLC30A7 localization with zinc concentration in subcellular compartments

• Temporal dynamics assessment:

  • Use time-course experiments with parallel samples for antibody detection and zinc measurement

  • Consider live-cell imaging with zinc sensors alongside fixed-cell antibody staining at matched timepoints