AMD1 Antibody
(Synonyms: AMD, AMD1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, SAMDC)Based on 1 Customer Validation
AMD1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to AMD1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, ICC/IF
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Reactivity :
Human, Mouse, Rat, Bovine
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Formulation:
Supplied in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|
| Dilution Ratio | 1:500-1000 | 1:50-200 |
Product Details
AMD1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to AMD1.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat, Bovine
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Observed Molecular WeightObserved band size: 34, 50 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 38 kDa
Synthetic peptide corresponding to the center region of human AMD1.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
AMD1 is essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels
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Isoforms & Post-Translational Modification
AMD1 has 2 isoforms, P17707-1: amino acid length is 334, molecular weight is 38340 Da (predicted); P17707-2: amino acid length is 186, molecular weight is 21301 Da (predicted).
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. -
Subunit
Heterotetramer of two alpha and two beta chains
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SwissProt ID
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Synonyms
AMD, AMD1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, SAMDC
Documentation