-Galactosidase Antibody Catalog Number: B2014930 (50 ug)
| Catalog number: | B2014930 |
| Lot number: | Batch Dependent |
| Expiration Date: | Batch dependent |
| Amount: | 50 ug |
| Molecular Weight or Concentration: | 200 g/ml |
| Supplied as: | N/A |
| Applications: | molecular tool for various biochemical applications |
| Storage: | 2-8oC |
| Keywords: | -Galactosidase Antibody |
| Grade: | Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um. |
-Galactosidase Antibody is offered in a defined 50ug package (Catalog B2014930) with a listed 200g/ml value under Molecular Weight or Concentration and storage noted as 28oC. The supplier positions this reagent as a molecular tool for various biochemical applications. Because the listing does not specify format details beyond Supplied as: N/A, this entry is best treated as a clearly documented antibody item whose core attributesamount, concentration field, storage, and keyword identityfacilitate straightforward SOP inclusion and inventory control in multi-user labs.
In common research workflows, antibodies to -galactosidase are used to verify the presence of -gal in samples tied to reporter systems or enzyme preparations, assemble capture/detection steps in qualitative immunoassays, or create control arms for training and platform checks. When the vendor does not prescribe a working dilution, it is sensible to determine conditions empirically for the matrix and platform at hand. Start with small pilot titrations, document buffer composition, incubation times, and time-at-temperature, and record lot identifiers so results are reproducible across runs and analysts. The concise specification set on this listing supports those documentation habits and helps teams harmonize handling across plates, membranes, or other bench setups.
Practical considerations include confirming background with the intended blocking and wash buffers, aligning secondary detection chemistry to the antibodys characteristics used in your lab, and tracking any stability notes under the stated 28oC storage. Within research-only boundaries, the clearly stated package size, the presence of a concentration entry, and the minimal but explicit application note make this -galactosidase antibody a straightforward, dependable component for labs standardizing -gal-related immunochemical workflows and exploratory assay development.
Why researchers choose this product:
- Defined 50ug package size for accurate documentation and inventory planning
- Listing includes a 200g/ml concentration entry to aid method setup and recording
- Specified storage at 28oC aligns with routine refrigerator handling
- Positioned as a molecular tool suitable for diverse biochemical workflows
- Concise, documentation-friendly fields (amount, concentration entry, storage, keywords, grade)
This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.
References
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- 4: Durbin H, Bodmer WF. A sensitive micro-immunoassay using beta-galactosidase/anti-beta-galactosidase complexes J Immunol Methods. 1987 Feb 26;97(1):19-27.
- 5: Franco D, de Boer PA, de Gier-de Vries C, Lamers WH, Moorman AF. Methods on in situ hybridization, immunohistochemistry and beta-galactosidase reporter gene detection Eur J Morphol. 2001 Jul;39(3):169-91.
- 6: Notkins AL. Polyreactive antibodies and polyreactive antigen-binding B (PAB) Cells Curr Top Microbiol Immunol. 2000;252:241-9.
- 7: Ishikawa E, Imagawa M, Hashida S, Yoshitake S, Hamaguchi Y, Ueno T. Enzyme-labeling of antibodies and their fragments for enzyme immunoassay and immunohistochemical staining J Immunoassay. 1983;4(3):209-327.
- 8: Yu Y, Fang L, Sun D. Biodistribution of HuCC49DeltaCH2-beta-galactosidase in colorectal cancer xenograft model Int J Pharm. 2010 Feb 15;386(1-2):208-15.
- 9: Franco D, de Boer PA, de Gier-de Vries C, Lamers WH, Moorman AF. Methods on in situ hybridization, immunohistochemistry and beta-galactosidase reporter gene detection Eur J Morphol. 2001 Feb;39(1):3-25.
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