SLC3A2 Rabbit Polyclonal Antibody

CAT#: TA365608

SLC3A2 rabbit polyclonal antibody

Product Images

Gel: 8%SDS-PAGE Lysate: 40 μg Lane 1-2: A375 and Jurkat cell lysates Primary antibody: TA365608 (SLC3A2 Antibody) at dilution 1/200 Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution Exposure time: 3 seconds

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  Immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using TA365608 (SLC3A2 Antibody) at dilution 1/40 (Original magnification: ×200)

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  Immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using TA365608 (SLC3A2 Antibody) at dilution 1/40, treated with fusion protein. (Original magnification: ×200)

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  Immunohistochemistry of paraffin-embedded Human liver cancer tissue using TA365608 (SLC3A2 Antibody) at dilution 1/40 (Original magnification: ×200)

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  Immunohistochemistry of paraffin-embedded Human liver cancer tissue using TA365608 (SLC3A2 Antibody) at dilution 1/40, treated with fusion protein. (Original magnification: ×200)

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Specifications

Product Data

• Applications: IHC, WB
• Recommended Dilution: WB: 500-2000
  WB positive control: A375 and Jurkat cell lysates
  IHC: 30-150
  Positive control: Human colorectal cancer
  Predicted cell location: Cytoplasm
• Reactivities: Human
• Host: Rabbit
• Isotype: IgG
• Clonality: Polyclonal
• Immunogen: Fusion protein of human SLC3A2
• Formulation: pH7.4 PBS, 0.05% NaN3, 40% Glycerol
• Concentration: lot specific
• Purification: Antigen affinity purification
• Conjugation: Unconjugated
• Storage: Store at -20°C.
• Stability: 1 year
• Predicted Protein Size: 68 kDa
• Database Link:
  UniProt ID P08195
• Background: This gene is a member of the solute carrier family and encodes a cell surface, transmembrane protein. The protein exists as the heavy chain of a heterodimer, covalently bound through di-sulfide bonds to one of several possible light chains. The encoded transporter plays a role in regulation of intracellular calcium levels and transports L-type amino acids. Alternatively spliced transcript variants, encoding different isoforms, have been characterized.