1
/
of
1
ELK Biotechnology
SKU:ES17025
DAD1 rabbit pAb
DAD1 rabbit pAb
Regular price
$250.00 USD
Regular price
Sale price
$250.00 USD
Unit price
/
per
Shipping calculated at checkout.
Couldn't load pickup availability
Applications: WB
Reactivity: Human; Mouse;Rat
Source: Rabbit
Dilution: WB 1:500-2000
Immunogen: Synthesized peptide derived from human DAD1 AA range: 38-88
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Concentration: 1 mg/ml
Human_gene_id: 1603
Human_swiss_prot_no: P61803
Subcellular_location: Endoplasmic reticulum membrane; Multi-pass membrane protein .
Background: DAD1, the defender against apoptotic cell death, was initially identified as a negative regulator of programmed cell death in the temperature sensitive tsBN7 cell line. The DAD1 protein disappeared in temperature-sensitive cells following a shift to the nonpermissive temperature, suggesting that loss of the DAD1 protein triggered apoptosis. DAD1 is believed to be a tightly associated subunit of oligosaccharyltransferase both in the intact membrane and in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes. [provided by RefSeq, Jul 2008],
Reactivity: Human; Mouse;Rat
Source: Rabbit
Dilution: WB 1:500-2000
Immunogen: Synthesized peptide derived from human DAD1 AA range: 38-88
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Concentration: 1 mg/ml
Human_gene_id: 1603
Human_swiss_prot_no: P61803
Subcellular_location: Endoplasmic reticulum membrane; Multi-pass membrane protein .
Background: DAD1, the defender against apoptotic cell death, was initially identified as a negative regulator of programmed cell death in the temperature sensitive tsBN7 cell line. The DAD1 protein disappeared in temperature-sensitive cells following a shift to the nonpermissive temperature, suggesting that loss of the DAD1 protein triggered apoptosis. DAD1 is believed to be a tightly associated subunit of oligosaccharyltransferase both in the intact membrane and in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes. [provided by RefSeq, Jul 2008],
Share
