TEX2 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
---|---|
Primary Accession | Q8IWB9 |
Other Accession | NP_060939.3 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 125303 Da |
Antigen Region | 571-599 aa |
Gene ID | 55852 |
---|---|
Other Names | Testis-expressed sequence 2 protein, Transmembrane protein 96, TEX2, KIAA1738, TMEM96 |
Target/Specificity | This TEX2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 571-599 amino acids from the Central region of human TEX2. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | TEX2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TEX2 |
---|---|
Synonyms | KIAA1738, TMEM96 |
Function | During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. |
Cellular Location | Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi- pass membrane protein. Note=Enriched at the nucleus- vacuole junction (PubMed:22250200). During endoplasmic reticulum (ER) stress, localizes to ER-Golgi contacts (By similarity) {ECO:0000250|UniProtKB:Q06833, ECO:0000269|PubMed:22250200} |
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Provided below are standard protocols that you may find useful for product applications.
Background
There are two isoforms.
References
Lee, I., et al. FASEB J. 20(2):202-206(2006)
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