• Immunohistochemistry of rat kidney with Anti-SLC25A5 primary antibody (STJ500087) at 1:100 dilution in Buffer. Section was treated with DAB and Haematoxylin stain. Magnification is at 40X.

Anti-SLC25A5 antibody (150-200) (STJ500087)

SKU:
STJ500087-100

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Host: Rabbit
Applications: CM/ELISA/ICC/IF/IHC/IP/WB
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-SLC25A5 (150-200) is suitable for use in Confocal Microscopy, ELISA, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Immunoprecipitation and Western Blot research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Purification: Affinity Purified
Concentration: 0.68 µg/µl
Dilution Range: WB: 1:500
DB: 1:10, 000
ELISA: 1:10, 000
IP: 1:200
IHC: 1:100
ICC: 1:100
IF: 1:100
CFM: 1:100
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: SLC25A5
Gene ID: 292
Uniprot ID: ADT2_HUMAN
Immunogen Region: 150-200
Immunogen: Synthetic peptide taken within amino acid region 150-200 on human ADP/ATP translocase
Tissue Specificity Expressed in erythrocytes (at protein level).
Post Translational Modifications Trimethylated by ANTKMT at Lys-52.
Function ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane. In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity. Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it. Probably mediates mitochondrial uncoupling in tissues that do not express UCP1. Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death. It is however unclear if SLC25A5/ANT2 constitutes a pore-forming component of mPTP or regulates it. Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation.
Protein Name Adp/Atp Translocase 2
Adp -Atp Carrier Protein 2
Adp -Atp Carrier Protein - Fibroblast Isoform
Adenine Nucleotide Translocator 2
Ant 2
Solute Carrier Family 25 Member 5 Cleaved Into - Adp/Atp Translocase 2 - N-Terminally Processed
Database Links Reactome: R-HSA-180897
Reactome: R-HSA-83936
Cellular Localisation Mitochondrion Inner Membrane
Multi-Pass Membrane Protein
Membrane
May Localize To Non-Mitochondrial Membranes
Alternative Antibody Names Anti-Adp/Atp Translocase 2 antibody
Anti-Adp -Atp Carrier Protein 2 antibody
Anti-Adp -Atp Carrier Protein - Fibroblast Isoform antibody
Anti-Adenine Nucleotide Translocator 2 antibody
Anti-Ant 2 antibody
Anti-Solute Carrier Family 25 Member 5 Cleaved Into - Adp/Atp Translocase 2 - N-Terminally Processed antibody
Anti-SLC25A5 antibody
Anti-AAC2 antibody
Anti-ANT2 antibody

Information sourced from Uniprot.org

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