TARP
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Official Full Name
TCR gamma alternate reading frame protein -
Overview
In some non-lymphoid tissues, the unrearranged T cell receptor gamma (TRG@) locus is expressed. The resulting transcript contains a subset of the TRG@ gene segments and is shorter than TRG@ transcripts expressed in lymphoid tissues. This RefSeq record represents the unrearranged TRG@ locus transcript; the complete TRG@ locus is represented by the genomic RefSeq NG_001336. The transcript represented by this RefSeq has two open reading frames (ORFs) that encode different proteins. The downstream ORF is in the same frame as TRG@ and its protein product is similar to TRG@ proteins. The upstream ORF uses a different reading frame and encodes a novel protein. -
Synonyms
TARP;TCR gamma alternate reading frame protein;T-cell receptor gamma-chain constant region;CD3G;TCRG;TCRGC1;TCRGC2
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
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Involved Pathway
TARP involved in several pathways and played different roles in them. We selected most pathways TARP participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with TARP were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
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Protein Function
TARP has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by TARP itself. We selected most functions TARP had, and list some proteins which have the same functions with TARP. You can find most of the proteins on our site.
| Function | Related Protein |
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Interacting Protein
TARP has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with TARP here. Most of them are supplied by our site. Hope this information will be useful for your research of TARP.
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References
- Zhu, SL; Feng, Y; et al. Identification of linear B-cell epitopes within Tarp of Chlamydia trachomatis. JOURNAL OF PEPTIDE SCIENCE 20:916-922(2014).
- Klueva, J; Gundelfinger, ED; et al. Intracellular Ca2+ and not the extracellular matrix determines surface dynamics of AMPA-type glutamate receptors on aspiny neurons. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES 369:-(2014).
