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ELK Biotechnology Syntaxin 1 rabbit pAb
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ELK Biotechnology Syntaxin 1 rabbit pAb

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Syntaxin 1 rabbit pAb는 신경계 특이 단백질 Syntaxin-1A를 인식하는 고품질 폴리클로날 항체입니다. WB, IHC, IF, ELISA 등 다양한 응용에 적합하며, 인간·마우스·랫·원숭이 시료에 반응합니다. 세포막 및 시냅스 소포 위치 연구에 유용합니다.

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pk
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ELK Biotechnology ES3537-100UL Syntaxin 1 rabbit pAb, 100UL pk판매 단위 pk ·
재고 확인 필요
402,000원VAT 포함 442,200원
ELK Biotechnology ES3537-50UL Syntaxin 1 rabbit pAb, 50UL pk판매 단위 pk ·
재고 확인 필요
301,000원VAT 포함 331,100원

ELK Biotechnology · ELK Biotechnology Syntaxin 1 rabbit pAb

Syntaxin 1 rabbit pAb

제품 정보

항목 내용
Product Name Syntaxin 1 rabbit pAb
Alternative Names STX1A; STX1; Syntaxin-1A; Neuron-specific antigen HPC-1
Applications WB; IHC; IF; ELISA
Recommended Dilutions Western Blot: 1/500 - 1/2000
Immunohistochemistry: 1/100 - 1/300
Immunofluorescence: 1/200 - 1/1000
ELISA: 1/20000
Not yet tested in other applications
Immunogen Synthesized peptide derived from human Syntaxin 1A (AA range: 1–50)
Host Rabbit
Storage -20°C / 1 year
Clonality Polyclonal
Isotype IgG
Concentration 1 mg/ml
Observed Band 35 kD
GeneID (Human) 6804
Human Swiss-Prot No. Q16623
Cellular Localization Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein; Cell junction, synapse, synaptosome; Cell membrane; Colocalizes with KCNB1 at the cell membrane; Isoform 2: Secreted
Species Reactivity Human; Mouse; Rat; Monkey

Background

This gene encodes a member of the syntaxin superfamily. Syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. They possess a single C-terminal transmembrane domain, a SNARE (Soluble NSF Attachment Protein Receptor) domain known as H3, and an N-terminal regulatory domain (Habc). Syntaxins bind synaptotagmin in a calcium-dependent manner and interact with voltage-dependent calcium and potassium channels via the C-terminal H3 domain. This gene product plays a key role in ion channel regulation and synaptic exocytosis. Alternatively spliced transcript variants encoding different isoforms have been identified.

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