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CARMA2 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, E |
|---|---|
| Primary Accession | Q9BXL6 |
| Other Accession | NP_077015, 332801087 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 113270 Da |
| Application Notes | CARMA2 antibody can be used for detection of CARMA2 by immunohistochemistry at 5 µg/mL. |
| Gene ID | 79092 |
|---|---|
| Other Names | CARMA2 Antibody: PRP, PSS1, BIMP2, CARMA2, PSORS2, Caspase recruitment domain-containing protein 14, CARD-containing MAGUK protein 2, Carma 2, caspase recruitment domain family, member 14 |
| Target/Specificity | CARD14; CARMA2 antibody is human specific. At least three isoforms of CARMA2 are known to exist; this antibody will only detect isoform 1. CARMA2 antibody is predicted not to cross-react with other CARMA proteins. |
| Reconstitution & Storage | CARMA2 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
| Precautions | CARMA2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | CARD14 |
|---|---|
| Synonyms | CARMA2 |
| Function | Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases (PubMed:11278692, PubMed:21302310, PubMed:27113748, PubMed:27071417). May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis. |
| Cellular Location | [Isoform 1]: Cytoplasm [Isoform 3]: Cytoplasm |
| Tissue Location | Isoform 1 is detected in placenta and epidermal keratinocytes (PubMed:22521418). Isoform 2 is detected in leukocytes and fetal brain (PubMed:22521418). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
CARMA2 Antibody: CARMA proteins belong to the membrane-associated guan-ylate kinase-like (MAGUK) family of proteins that can function as molecular scaffolds that assist assembly of signal transduction molecules. CARMA1, CARMA2, and CARMA3 share high degrees of sequence and functional homology, but their tissue-specific distribution suggests that they serve distinct biological functions in different cell types. As with CARMA1, the CARD domain of CARMA2 has been shown to specifically interact with BCL10, a protein known to function as a positive regulator of cell apoptosis and NF-κB activation. When expressed in cells, this protein activated NF-κB and induced the phosphorylation of BCL10 Alternative splicing of CARMA2 results in isoforms that possess differential effects on NF-κB activation and endoplasmic reticulum stress-induced cell death.
References
Fanning AS and Anderson JM. Protein modules as organizers of membrane structure. Curr. Opin. Cell Biol. 1999; 11:432-9.
Gaide O, Martinon F, Michau O, et al. Carma1, 1 CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappa B activation. FEBS Lett. 2001; 496:121-7.
Bertin J, Wang L, Guo Y, et al. CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B. J. Biol. Chem. 2001; 276:11877-82.
Scudiero I, Zotti T, Ferravante A, et al. Alternative splicing of CARMA2/CARD14 transcripts generates protein variants with differential effect on NF-kB activation endoplasmic reticulum stress-induced cell death. J. Cell Physiol. 2011; 226:3121-31.
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