You Searched For: tom

Catalog Number: (75933-014)

Supplier: Rockland Immunochemical

Description: The translocase of outer mitochondrial membrane (TOM) complex is a multisubunit complex involved in the recognition, unfolding, and translocation of preproteins into the mitochondria. TOM70, an important member of the TOM complex, contains a tetratricopeptide repeat domain similar to those found in cytosolic chaperones such as Hsp90 and Hsc70 and provides a docking site for these proteins. This interaction is thought to be a critical first step in the TOM70-dependent mitochondrial import, followed by contact between the preprotein and TOM70. After targeting to TOM70, preproteins are translocated through the outer membrane via the TOM40 import pore complex. The precise mechanism of how preproteins progress from TOM70 to TOM40 to full translocation is still unclear. At least two isoforms of TOM70 are known to exist.

Catalog Number: (75933-016)

Supplier: Rockland Immunochemical

Description: The translocase of outer mitochondrial membrane (TOM) complex is a multisubunit complex involved in the recognition, unfolding, and translocation of preproteins into the mitochondria. TOM70, an important member of the TOM complex, contains a tetratricopeptide repeat domain similar to those found in cytosolic chaperones such as Hsp90 and Hsc70 and provides a docking site for these proteins. This interaction is thought to be a critical first step in the TOM70-dependent mitochondrial import, followed by contact between the preprotein and TOM70. After targeting to TOM70, preproteins are translocated through the outer membrane via the TOM40 import pore complex. The precise mechanism of how preproteins progress from TOM70 to TOM40 to full translocation is still unclear. At least two isoforms of TOM70 are known to exist.

Catalog Number: (10750-378)

Supplier: Prosci

Description: TOM70 Antibody: The translocase of outer mitochondrial membrane (TOM) complex is a multisubunit complex involved in the recognition, unfolding, and translocation of preproteins into the mitochondria. TOM70, an important member of the TOM complex, contains a tetratricopeptide repeat domain similar to those found in cytosolic chaperones such as Hsp90 and Hsc70 and provides a docking site for these proteins. This interaction is thought to be a critical first step in the TOM70-dependent mitochondrial import, followed by contact between the preprotein and TOM70. After targeting to TOM70, preproteins are translocated through the outer membrane via the TOM40 import pore complex. The precise mechanism of how preproteins progress from TOM70 to TOM40 to full translocation is still unclear. At least two isoforms of TOM70 are known to exist.

Catalog Number: (103444-858)

Supplier: Affymetrix, Inc.

Description: A suggested positive control is 293 cell lysate. PA5-20664 can be used with blocking peptide PEP-0784. The translocase of outer mitochondrial membrane (TOM) complex is a multisubunit complex involved in the recognition, unfolding, and translocation of preproteins into the mitochondria. TOM70, an important member of the TOM complex, contains a tetratricopeptide repeat domain similar to those found in cytosolic chaperones such as Hsp90 and Hsc70 and provides a docking site for these proteins. This interaction is thought to be a critical first step in the TOM70-dependent mitochondrial import, followed by contact between the preprotein and TOM70. After targeting to TOM70, preproteins are translocated through the outer membrane via the TOM40 import pore complex. The precise mechanism of how preproteins progress from TOM70 to TOM40 to full translocation is still unclear. At least two isoforms of TOM70 are known to exist.

Catalog Number: (10750-368)

Supplier: Prosci

Description: TOM70 Antibody: The translocase of outer mitochondrial membrane (TOM) complex is a multisubunit complex involved in the recognition, unfolding, and translocation of preproteins into the mitochondria. TOM70, an important member of the TOM complex, contains a tetratricopeptide repeat domain similar to those found in cytosolic chaperones such as Hsp90 and Hsc70 and provides a docking site for these proteins. This interaction is thought to be a critical first step in the TOM70-dependent mitochondrial import, followed by contact between the preprotein and TOM70. After targeting to TOM70, preproteins are translocated through the outer membrane via the TOM40 import pore complex. The precise mechanism of how preproteins progress from TOM70 to TOM40 to full translocation is still unclear.

Catalog Number: (10801-894)

Supplier: Rockland Immunochemical

Description: ARAF belongs to the RAF subfamily of the Ser/Thr protein kinase family, and maybe involved in cell growth and development. ARAF play a critical role in cell growth and development (1).The N-terminal regulatory domain of ARAF interacted with the putative mitochondrial proteins TOM and TIM44. ARAF is expressed predominantly in urogenital tissues (2). The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus. ARAF Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, and Cancer research.

Catalog Number: (103664-720)

Supplier: Sino Biological

Description: A DNA sequence encoding the mouse TMEFF1 (EDL02331.1) (Met1-Val323) was expressed with the Fc region of human IgG1 at the C-terminus.

Catalog Number: (103461-470)

Supplier: Affymetrix, Inc.

Description: MA1-20161 detects TOMM22 in human and non-human primate samples. MA1-20161 has been successfully used in immunocytochemistry and Western blot procedures. The MA1-20161 immunogen is a membrane fraction from Vero (monkey kidney-derived) cells. TOM22 has a negatively charged N-terminal region exposed to the cytosol, a putative transmembrane region, and a C-terminal intermembrane space region with little negative charge. The following functions can be assigned to the three domains of TOM22: the cytosolic N-terminal domain plays a dual role, specifically important for presequence binding; the intermembrane space domain provides a trans binding site for presequences, and the single membrane anchor of TOM22 is crucial for the integrity of the GIP (general import gene) complex. The TOM complex of mammalian mitochondria resembles the fungal TOM complex, but is distinct from the plant TOM system. Thus, while unique components of the mammalian mitochondrial import system have been identified (e.g. TOM34 and metaxin), TOM22, and TOM37 have not been identified in plant mitochondria.

Catalog Number: (103444-838)

Supplier: Affymetrix, Inc.

Description: A suggested positive control is rat brain tissue lysate. PA5-20654 can be used with blocking peptide PEP-0774. The translocase of outer mitochondrial membrane (TOM) complex is a multisubunit complex involved in the recognition, unfolding, and translocation of preproteins into the mitochondria. TOM70, an important member of the TOM complex, contains a tetratricopeptide repeat domain similar to those found in cytosolic chaperones such as Hsp90 and Hsc70 and provides a docking site for these proteins. This interaction is thought to be a critical first step in the TOM70-dependent mitochondrial import, followed by contact between the preprotein and TOM70. After targeting to TOM70, preproteins are translocated through the outer membrane via the TOM40 import pore complex. The precise mechanism of how preproteins progress from TOM70 to TOM40 to full translocation is still unclear. At least two isoforms of TOM70 are known to exist.

Catalog Number: (103485-142)

Supplier: Affymetrix, Inc.

Description: Suggested positive control: purified mitochondrial extracts and HeLa whole cell extract. Functional mitochondria require up to 1000 proteins to function properly, with 99% synthesized as precursors in the cytoplasm and transported into the mitochondria with the aid of cytosolic chaperones and mitochondrial translocators (import components). Proteins to be imported are chaperoned to the mitochondria by the cytosolic heat shock protein (cHSP70) and are immediately pursued by Translocators of the Outer Membrane (TOMs), followed by transient interactions of the unfolded proteins with Translocators of the Inner Membrane (TIMs). TOMM70A is ubiquitously expressed in human tissues and localizes in the mitochondria. TOMM70A could play a significant role in the import of nuclear-encoded mitochondrial proteins with internal targeting sites such as ADP/ATP carriers and the uncoupling proteins.

Catalog Number: (10273-170)

Supplier: Proteintech

Description: The PRPF6 antibody from Proteintech is a rabbit polyclonal antibody to a fusion protein of human PRPF6. This antibody recognizes human, mouse antigen. The PRPF6 antibody has been validated for the following applications: ELISA, WB, IHC analysis.

Catalog Number: (103426-234)

Supplier: Affymetrix, Inc.

Description: This Antibody targets PRP6 in WB applications and shows reactivity with Human samples. The immunogen is recombinant fragment corresponding to a region within amino acids 495 and 830 of Human PRP6. The protein encoded by this gene appears to be involved in pre-mRNA splicing, possibly acting as a bridging factor between U5 and U4/U6 snRNPs in formation of the spliceosome. The encoded protein also can bind androgen receptor, providing a link between transcriptional activation and splicing.

Catalog Number: (10261-272)

Supplier: Bioss

Description: The majority of mitochondrial-directed proteins are encoded by the nuclear genome and are transported to the mitochondria via regulated processes involving the mitochondrial Tom and Tim proteins (1). The mitochondrial Tim protein family is comprised of a large group of evolutionarily conserved proteins that are found in most eukaryotes (1,2). Import of nuclear-encoded precursor proteins into and across the mitochondrial inner membrane is mediated by two distinct complexes, the Tim23 complex and the Tim22 complex, which differ in their substrate specificity (1). Defects in Tim proteins are implicated in several neuro-degenerative diseases, suggesting important roles for Tim proteins in development and health (3,4). Tim8A and Tim8B, which map to human chromosomes Xq22.1 and 11q23.1-q23.2, respectively, are conserved proteins of the mitochondrial intermembrane space, which are organized in hetero-oligomeric complex with Tim13 (5,6,7). Tim8A is highly expressed in fetal and adult brain (5). Tim8A is mutated in deafness dystonia syndrome, a novel type of disease that causes severe neurological defects, thought to be caused by a defective mitochondrial protein transport system (5,8).

Catalog Number: (10261-276)

Supplier: Bioss

Description: The majority of mitochondrial-directed proteins are encoded by the nuclear genome and are transported to the mitochondria via regulated processes involving the mitochondrial Tom and Tim proteins (1). The mitochondrial Tim protein family is comprised of a large group of evolutionarily conserved proteins that are found in most eukaryotes (1,2). Import of nuclear-encoded precursor proteins into and across the mitochondrial inner membrane is mediated by two distinct complexes, the Tim23 complex and the Tim22 complex, which differ in their substrate specificity (1). Defects in Tim proteins are implicated in several neuro-degenerative diseases, suggesting important roles for Tim proteins in development and health (3,4). Tim8A and Tim8B, which map to human chromosomes Xq22.1 and 11q23.1-q23.2, respectively, are conserved proteins of the mitochondrial intermembrane space, which are organized in hetero-oligomeric complex with Tim13 (5,6,7). Tim8A is highly expressed in fetal and adult brain (5). Tim8A is mutated in deafness dystonia syndrome, a novel type of disease that causes severe neurological defects, thought to be caused by a defective mitochondrial protein transport system (5,8).

Catalog Number: (10266-534)

Supplier: Bioss

Description: The majority of mitochondrial-directed proteins are encoded by the nuclear genome and are transported to the mitochondria via regulated processes involving the mitochondrial Tom and Tim proteins (1). The mitochondrial Tim protein family is comprised of a large group of evolutionarily conserved proteins that are found in most eukaryotes (1,2). Import of nuclear-encoded precursor proteins into and across the mitochondrial inner membrane is mediated by two distinct complexes, the Tim23 complex and the Tim22 complex, which differ in their substrate specificity (1). Defects in Tim proteins are implicated in several neuro-degenerative diseases, suggesting important roles for Tim proteins in development and health (3,4). Tim8A and Tim8B, which map to human chromosomes Xq22.1 and 11q23.1-q23.2, respectively, are conserved proteins of the mitochondrial intermembrane space, which are organized in hetero-oligomeric complex with Tim13 (5,6,7). Tim8A is highly expressed in fetal and adult brain (5). Tim8A is mutated in deafness dystonia syndrome, a novel type of disease that causes severe neurological defects, thought to be caused by a defective mitochondrial protein transport system (5,8).

Catalog Number: (10261-274)

Supplier: Bioss

Description: The majority of mitochondrial-directed proteins are encoded by the nuclear genome and are transported to the mitochondria via regulated processes involving the mitochondrial Tom and Tim proteins (1). The mitochondrial Tim protein family is comprised of a large group of evolutionarily conserved proteins that are found in most eukaryotes (1,2). Import of nuclear-encoded precursor proteins into and across the mitochondrial inner membrane is mediated by two distinct complexes, the Tim23 complex and the Tim22 complex, which differ in their substrate specificity (1). Defects in Tim proteins are implicated in several neuro-degenerative diseases, suggesting important roles for Tim proteins in development and health (3,4). Tim8A and Tim8B, which map to human chromosomes Xq22.1 and 11q23.1-q23.2, respectively, are conserved proteins of the mitochondrial intermembrane space, which are organized in hetero-oligomeric complex with Tim13 (5,6,7). Tim8A is highly expressed in fetal and adult brain (5). Tim8A is mutated in deafness dystonia syndrome, a novel type of disease that causes severe neurological defects, thought to be caused by a defective mitochondrial protein transport system (5,8).