Rabbit Anti-Human TESPA1 (a.a. 177-521) Polyclonal antibody

Name: Rabbit Anti-Human TESPA1 (a.a. 177-521) Polyclonal antibody
SKU: DPABH-20873
Rating: 5 (1 reviews)

Rabbit Anti-Human TESPA1 (a.a. 177-521) Polyclonal antibody for WB, ELISA

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COA

SDS

Datasheet

Key features and details

Target: Human TESPA1
Host: Rabbit
Application: WB, ELISA
Species Reactivity: Human

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

Recombinant human KIAA0748 protein; Source: E. coli derived, PET30a; Tag: 6*His; Domain: 177-521 aa of BC132732

Conjugate

Unconjugated

Applications

Application Notes

WB: 1:500-1:2000

General Notes

This product (Catalog No. DPABH-20873) is a rabbit-derived polyclonal antibody raised against human TESPA1, targeting the amino acid region 177–521 of the protein. It has been affinity purified by Protein A. TESPA1, or thymocyte expressed, positive selection associated 1, is a protein-coding gene in humans that encodes a protein essential for the development and maturation of T cells, particularly during the late stages of thymocyte differentiation in the thymus. Located on the long arm of chromosome 12 at cytogenetic band 12q13.2, the TESPA1 gene spans approximately 37 kb and consists of 16 exons, producing multiple protein isoforms through alternative splicing, with the longest isoform comprising 423 amino acids. The TESPA1 protein is a component of both the T cell receptor (TCR) signalosome and the COP9 signalosome, where it facilitates TCR-mediated signaling pathways critical for positive selection of thymocytes and overall T cell homeostasis. It contains a conserved KRAP_IP3R_bind domain that enables interactions with inositol 1,4,5-trisphosphate receptors (IP3Rs), thereby regulating intracellular calcium flux in response to TCR stimulation. Expression of TESPA1 is biased toward immune tissues, with high levels observed in lymph nodes and brain (both RPKM 4.0) and expression in other tissues such as spleen and thymus, reflecting its role in adaptive immunity. Post-translational modifications, including phosphorylation triggered by store-operated calcium entry, further modulate its function in T cell activation and signaling. The protein is localized primarily in the cytosol, cytoplasm, and endoplasmic reticulum membrane, positioning it to influence mitochondrial-associated endoplasmic reticulum membranes and calcium homeostasis.
DPABH-20873 is suitable for use in Western blot (WB) (1:500–1:2,000) application.
DPABH-20873 is supplied as a liquid formulation in PBS with 0.02% sodium azide and 50% glycerol, pH 7.3. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.

Target

Alternative Names

HSPC257; KIAA0748; TESPA1; thymocyte expressed, positive selection associated 1

Entrez Gene ID

9840

UniProt ID

A2RU30

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling

NATURE IMMUNOLOGY

Authors: Wang, Di; Zheng, Mingzhu; Lei, Lei; Ji, Jian; Yao, Yunliang; Qiu, Yuanjun; Ma, Lie; Lou, Jun; Ouyang, Chuan; Zhang, Xue; He, Yuewei; Chi, Jun; Wang, Lie; Kuang, Ying; Wang, Jianli; Cao, Xuetao; Lu, Linrong

Abstract

Signaling via the T cell antigen receptor (TCR) during the CD4(+)CD8(+) double-positive developmental stage determines thymocyte selection and lineage commitment. Here we describe a previously uncharacterized T cell-expressed protein, Tespa1, with critical functions during the positive selection of thymocytes. Tespa1(-/-) mice had fewer mature thymic CD4(+) and CD8(+) T cells, which reflected impaired thymocyte development. Tespa1 associated with the TCR signaling components PLC-gamma 1 and Grb2, and Tespa1 deficiency resulted in attenuated TCR signaling, as reflected by defective activation of the Erk-AP-1 and Ca2+-NFAT pathways. Our findings demonstrate that Tespa1 is a component of the TCR signalosome and is essential for T cell selection and maturation through the regulation of TCR signaling during T cell development.

Tespa1 protein is phosphorylated in response to store-operated calcium entry

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Fujimoto, Takahiro; Matsuzaki, Hiroshi; Tanaka, Masatoshi; Shirasawa, Senji

Abstract

We previously reported that Tespa1 (thymocyte-expressed, positive selection-associated gene 1) protein expressed in lymphocytes physically interacts with IP3R (Inositol 1,4,5-trisphosphate receptor), a Ca2+ channel protein spanning endoplasmic reticulum (ER) membrane. However, the biochemical characterization of Tespa1 protein remains unknown. In this study, we have found that Tespa1 protein was posttranslationally modified upon intracellular Ca2+ increase in thymocytes. Through the analyses using various inhibitors, store-operated Ca2+ entry (SOCE) was found to be an essential factor for the Tespa1 protein modification induced by T cell receptor (TCR)-stimulation. Remarkably, the Ca2+-dependent Tespa1 protein modification was restored by in vitro protein phosphatase treatment, indicating that this modification was due to phosphorylation. Moreover, we examined whether Ca2+-dependent phosphorylation of Tespa1 protein would affect the physical association between Tespa1 and IP3R proteins, revealing that physical association of these proteins is maintained regardless of the presence or absence of phosphorylation of Tespa1. In addition, KRAP protein which represents substantial amino acid sequence homology to Tespa1 was also posttranslationally phosphorylated by intracellular Ca2+ increase in HCT116 human colon cancer cells and HEK293 human embryonic kidney cells, suggesting that common signaling mechanism(s) may contribute to the molecular modification of Tespa1 and KRAP in different cellular processes. All these results suggested a novel molecular modification of Tespa1 and the existence of the regulatory pathway that SOCE affects the Tespa1-IP3R molecular complex. (C) 2013 Elsevier Inc. All rights reserved.