Recombinant; Rabbit anti Human Lysozyme Antibody; WB, ICC, IF; Unconjugated
| SKU | Size | Availability | Price | Qty |
|---|---|---|---|---|
| Ab113835-10μl | 10μl | In stock | $69.90 | |
| Ab113835-50μl | 50μl | In stock | $209.90 | |
| Ab113835-100μl | 100μl | Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding. | $339.90 | |
| Ab113835-1ml | 1ml | Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding. | $2,399.90 |
Recombinant; Rabbit anti Human Lysozyme Antibody; WB, ICC, IF; Unconjugated
| Product Name | Recombinant Lysozyme Antibody - Primary antibody, specific to Lysozyme, Rabbit IgG |
|---|---|
| Synonyms | 1 4 beta N acetylmuramidase C antibody; 1 antibody; 4-beta-N-acetylmuramidase C antibody; EC 3.2.1.17 antibody; LYSC_HUMAN antibody; Lysosyme antibody; Lysozyme (renal amyloidosis) antibody; Lysozyme C antibody; Lysozyme C precursor antibody; LYZ antibody |
| Specifications & Purity | ExactAb™, Validated, Recombinant |
| Host species | Rabbit |
| Specificity | Lysozyme |
| Immunogen | A synthetic peptide derived from human Lysozyme (AA 134-145) |
| Positive Control | WB: Human milk and U937 lysates. ICC/IF: Hep G2 cells. |
| Conjugation | Unconjugated |
| Grade | ExactAb™, Recombinant, Validated |
| Product Description | Rabbit anti Human Lysozyme Antibody, Recombinant, could be used for WB, ICC/IF and so on. |
| Isotype | Rabbit IgG |
|---|---|
| SDS-PAGE | 150 kDa |
| Purification Method | Antigen affinity purified |
| Form | Liquid |
| Storage Temp | Store at -20°C,Avoid repeated freezing and thawing |
| Shipped In | Ice chest + Ice pads |
| Stability And Storage | Store at 4℃ short term (1-2 weeks). Store at -20℃ long term (24 months). Upon delivery aliquot. Avoid freeze/thaw cycle. |
Recombinant Lysozyme Antibody (Ab113835) - Western Blot
All lanes: Recombinant Lysozyme Antibody (Ab113835) at 1/2000 dilution
Samples: Lysates at 20 µg per lane
Secondary: Goat Anti-Rabbit IgG H&L (HRP) (Ab170144) at 1/20000 dilution
Predicted band size: 17 kDa
Observed band size: 15 kDa
Exposure time: 1.0 s
Recombinant Lysozyme Antibody (Ab113835) - Western Blot
All lanes: Recombinant Lysozyme Antibody (Ab113835) at 1/1000 dilution
Samples: Lysates at 20 µL per lane
Secondary: Goat Anti-Rabbit IgG H&L (HRP) (Ab170144) at 1/30000 dilution
Predicted band size: 17 kDa
Observed band size: 15 kDa
Exposure time: 21.9 s
Recombinant Lysozyme Antibody (Ab113835) - IF/ICC
Immunocytochemistry analysis of Lysozyme (green) in Hep G2 using Recombinant Lysozyme Antibody (Ab113835), and cells were counterstained with DAPI (blue).
| Activity Type | Activity Value -log(M) | Mechanism of Action | Activity Reference | Publications (PubMed IDs) |
|---|
| Application | Dilution info |
|---|---|
| WB | 1/500-1/2000 |
| ICC/IF |
1/50-1/200
|
Enter Lot Number to search for COA:
To view the certificate results,please click on a Lot number.For Lot numbers from past orders,please use our order status section
| Lot Number | Certificate Type | Date | Item |
|---|---|---|---|
 ZJ24F0202862 | Certificate of Analysis | Feb 23, 2024 | Ab113835 |
| ZJ24F0202861 | Certificate of Analysis | Feb 23, 2024 | Ab113835 |
| 1. Ohkubo, T T, Taniyama, Y Y and Kikuchi, M M.. (1991) 1H and 15N NMR study of human lysozyme.. Journal of biochemistry, [PMID:1794972] |
| 2. Inaka, K K, Taniyama, Y Y, Kikuchi, M M, Morikawa, K K and Matsushima, M M.. (1991) The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast.. The Journal of biological chemistry, (5): [PMID:2061330] |
| 3. Redfield, C C and Dobson, C M CM.. (1990) 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme.. Biochemistry, (7): [PMID:2207098] |
| 4. Peters, C W CW, Kruse, U U, Pollwein, R R, Grzeschik, K H KH and Sippel, A E AE.. (1989) The human lysozyme gene. Sequence organization and chromosomal localization.. European journal of biochemistry, (1): [PMID:2546758] |
| 5. Yoshimura, K K, Toibana, A A and Nakahama, K K.. (1988) Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae.. Biochemical and biophysical research communications, (29): [PMID:2829884] |
| 6. Castañón, M J MJ, Spevak, W W, Adolf, G R GR, Chlebowicz-Sledziewska, E E and Sledziewski, A A.. (1988) Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae.. Gene, (30): [PMID:2971592] |
| 7. Chung, L P LP, Keshav, S S and Gordon, S S.. (1988) Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells.. Proceedings of the National Academy of Sciences of the United States of America, [PMID:3413092] |
| 8. Jollés, J J and Jollés, P P.. (1971) Human milk lysozyme: unpublished data concerning the establishment of the complete primary structure; comparison with lysozymes of various origins.. Helvetica chimica acta, [PMID:5168859] |
| 9. Canfield, R E RE, Kammerman, S S, Sobel, J H JH and Morgan, F J FJ.. (1971) Primary structure of lysozymes from man and goose.. Nature: New biology, (7): [PMID:5284421] |
| 10. Blake, C C CC, Pulford, W C WC and Artymiuk, P J PJ.. (1983) X-ray studies of water in crystals of lysozyme.. Journal of molecular biology, (5): [PMID:6876162] |
| 11. Artymiuk, P J PJ and Blake, C C CC.. (1981) Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions.. Journal of molecular biology, (15): [PMID:7334520] |
| 12. Pepys, M B MB and 9 more authors.. (1993) Human lysozyme gene mutations cause hereditary systemic amyloidosis.. Nature, (8): [PMID:8464497] |
| 13. Kanaya, E E, Ishihara, K K, Tsunasawa, S S, Nokihara, K K and Kikuchi, M M.. (1993) Indication of possible post-translational formation of disulphide bonds in the beta-sheet domain of human lysozyme.. The Biochemical journal, (1): [PMID:8503881] |
| 14. and Steinrauf, L K LK.. (1998) Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A.. Acta crystallographica. Section D, Biological crystallography, (1): [PMID:9757091] |
| 15. Jollès, J J and Jollès, P P.. (1972) Comparison between human and bird lysozymes: Note concerning the previously observed deletion.. FEBS letters, (15): [PMID:11946553] |
| 16. Thomsen, J J, Lund, E H. EH, Kristiansen, K K, Brunfeldt, K K and Malmquist, J J.. (1972) A val-val sequence found in a human monocytic leukemia lysozyme.. FEBS letters, (15): [PMID:11946554] |
