LS-C355233
antibody from LSBio
Targeting: SERPINA1
A1A, A1AT, AAT, alpha-1-antitrypsin, alpha1AT, PI, PI1
Antibody data
- Antibody Data
- Antigen structure
- References [0]
- Comments [0]
- Validations
- Western blot [2]
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Validation data
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- Product number
- LS-C355233 - Provider product page
- Provider
- LSBio
- Product name
- SERPINA1 / Alpha 1 Antitrypsin Antibody (clone TMF1#4B5) LS-C355233
- Antibody type
- Monoclonal
- Description
- Protein A purified
- Reactivity
- Human
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- TMF1#4B5
- Storage
- Short term: store at 4°C. Long term: aliquot and store at -20°C. Avoid freeze-thaw cycles.
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Supportive validation
- Submitted by
- LSBio (provider)
- Main image
- Experimental details
- Western blot analysis of Alpha1-Antitrypsin was performed using membrane enriched extracts (30 ug lysate) of Hep G2 (Lane 1) and tissue extract of Mouse Liver (Lane 2). The blots were probed with Anti-Alpha1-Antitrypsin Mouse Monoclonal Antibody and detected by chemiluminescence using Goat anti-Mouse IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 47 kDa band corresponding to Alpha1-Antitrypsin was observed across the cell line and tissue tested. Known quantity of protein samples were electrophoresed using 10 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5 % skimmed milk.
- Submitted by
- LSBio (provider)
- Main image
- Experimental details
- Western blot analysis was performed on membrane enriched extracts (30 ug) of (Fig 1) HT-29 (Lane 1) and Hep G2 (Lane 2).Likewise, Western blot analysis was performed on (Fig 2) condition media of Hep G2 (Lane 1), PC3 (Lane 2) and HeLa (Lane 3).The blots were probed with Anti-Alpha1-Antitrypsin Mouse Monoclonal Antibody and detected by chemiluminescence using Goat anti-Mouse IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. In Figure 1, a ~47 kDa band corresponding Alpha1-Antitrypsin was observed in Hep G2, and a ~55kDa band was observed in HT-29 due to glycosylation of protein. Also, in Figure 2, ~60kDa bands were observed in Hep G2, PC 3 and HeLa due to glycosylation of protein. Known quantity of protein samples were electrophoresed using4-12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody using iBind Flex Western Starter Kit.