Invitrogen

Human TID1 (aa 181-274) Control Fragment Recombinant Protein

Product Details

RP-98662

Applications

Tested Dilution

Publications

Control (Ctrl)

Assay-dependent

Blocking Assay (BLOCK)

Assay-dependent

Product Specifications

Species

Human

Expression System

E. coli

Amino acid sequence

DPEELFRKIFGEFSSSSFGDFQTVFDQPQEYFMELTFNQAAKGVNKEFTVNIMDTCERCNGKGNEPGTKVQHCHYCGGSGMETINTGPFVMRST

Tag

His-ABP-tag

Class

Recombinant

Type

Protein

Purity

>80% by SDS-PAGE and Coomassie blue staining

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

≥5.0 mg/mL

Purification

purified

Storage buffer

1M urea/PBS, pH 7.4

Contains

no preservative

Storage conditions

-20°C, Avoid Freeze/Thaw Cycles

Product Specific Information

Highest antigen sequence indentity to the following orthologs: Mouse (96%), Rat (96%).

This recombinant protein control fragment may be used for blocking experiments with the corresponding antibody, PA5-83522. In IHC/ICC and WB experiments, we recommend a 100x molar excess of the protein fragment control based on the concentration and the molecular weight. Pre-incubate the antibody-protein control fragment mixture for 30 min at room temperature.

Target Information

TID1 is a human homolog of the Drosophila tumor suppressor lethal (2) tumorous imaginal discs, l(2)tid and encodes two mitochondrial matrix localized splice variants of human Tid-1 designated hTid-1S and hTid-1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperones for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid-1L increases apoptosis induced by DNA damaging agents as mitomycin-C and TNF-a. A J-domain mutant of hTid-1L can dominantly suppress apoptosis and in sharp contrast the J-domain mutant of hTid-1S increases apoptosis. Expression of hTid-1S and hTid-1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti- and pro- apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: DnaJ (Hsp40) homolog, subfamily A, member 3; DnaJ homolog subfamily A member 3, mitochondrial; DnaJ protein Tid-1; Hepatocellular carcinoma-associated antigen 57; hTid-1; Tumorous imaginal discs protein Tid56 homolog