HSN1 Antibody
(Synonyms: LCB1, SPTLC1, Serine palmitoyltransferase 1, Long chain base biosynthesis protein 1, Serine-palmitoyl-CoA transferase 1, LCB 1, SPT 1, SPT1)HSN1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to HSN1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:50-200 |
Product Details
HSN1 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to HSN1.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 53 kDa
Note: 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: 52 kDa
Synthetic peptide corresponding to the C-term region of human HSN1.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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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
HSN1 is a Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2 or SPTLC3 forms the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. Required for adipocyte cell viability and metabolic homeostasis (By similarity)[1][2][3][4][5].
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Subcellular Localization
Endoplasmic reticulum membrane
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Expression
Tissue_Specificity: Widely expressed. Not detected in small intestine.
Induction: Expression at protein level is highly increased in brains of patients with Alzheimer disease. No changes are observed at mRNA level. -
Isoforms & Post-Translational Modification
HSN1 has 2 isoforms, O15269-1: amino acid length is 473, molecular weight is 52744 Da (predicted); O15269-2: amino acid length is 143, molecular weight is 16073 Da (predicted).
Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. -
Subunit
Component of the serine palmitoyltransferase (SPT) complex, which is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB.
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SwissProt ID
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Synonyms
LCB1, SPTLC1, Serine palmitoyltransferase 1, Long chain base biosynthesis protein 1, Serine-palmitoyl-CoA transferase 1, LCB 1, SPT 1, SPT1
Documentation
[1]. Han G, et al. Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. [Content Brief]
[2]. Li S, et al. Structural insights into the assembly and substrate selectivity of human SPT-ORMDL3 complex. Nat Struct Mol Biol. 2021 Mar;28(3):249-257. [Content Brief]
[3]. Spears ME, et al. De novo sphingolipid biosynthesis necessitates detoxification in cancer cells. Cell Rep. 2022 Sep 27;40(13):111415. [Content Brief]
[4]. Hornemann T, et al. The SPTLC3 subunit of serine palmitoyltransferase generates short chain sphingoid bases. J Biol Chem. 2009 Sep 25;284(39):26322-30. [Content Brief]
[5]. Wang Y, et al. Structural insights into the regulation of human serine palmitoyltransferase complexes. Nat Struct Mol Biol. 2021 Mar;28(3):240-248. [Content Brief]
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