
ASAH1 Polyklonale Antilichaam, APC-Cy7 Vervoeging
Kwaliteit
ISO Gecertificeerd
Levering
24-48 uur
Technische Specificaties
Acid ceramidase catalyzes the degradation of ceramide in normal tissues, and deficiency leads to accumulation of ceramide in tissues, a hallmark of Farber disease. Effected individuals experience early onset joint problems and neurological problems, owing to mutations in the acid ceramidase gene. Bioinformatic analysis of gene expression also reveals acid ceramidase to be among the 5 most important genes associated with melanoma. In addition to ceramide hydrolysis, purified acid ceramidase also exhibits the ability to catalyze ceramide synthesis, utilizing [14C]lauric acid and sphingosine as substrates. Interestingly, pH regulates which reaction is favored; for hydrolysis the pH optimum is 4.5, whereas for the reverse reaction favors a pH of 5.5, further supporting a complex and central role for acid ceramidase in sphingolipid metabolism.
AC; ACDase; Acid CDase; Acid ceramidase; Acid ceramidase precursor; Acid ceramidase subunit beta; Acylsphingosine deacylase; ASAH 1; ASAH; ASAH1; ASAH1_HUMAN; FLJ21558; FLJ22079; N acylsphingosine amidohydrolase acid ceramidase 1; N acylsphingosine amidohydrolase 1; N acylsphingosine amidohydrolase; N-acylsphingosine amidohydrolase; PHP; PHP32; Putative 32 kDa heart protein.
427
Cytoplasm
• Rabbit
Mouse
301-395/395
ASAH1
• Polyclonal
• IgG
APC-Cy7
KLH conjugated synthetic peptide derived from human Acid ceramidase subunit beta
WB, IF (IHC-P), IF (IHC-F), IF (ICC)
Purified by Protein A.
650nm/780nm
1µg/µl
WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)
Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Unmodified
Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.
427
Human, Rat, Dog, Cow, Sheep, Pig, Horse, Chicken
Beschrijving
ASAH1 Polyklonale Antilichaam, APC-Cy7 Vervoeging Beschikbaar in 100 µL. Bestel eenvoudig online met snelle levering.
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