SH2D1A Antibody [C12N16] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 FCM1:400

Application
WB, FCM

Reactivity
Human

Source
Rat Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
14 kDa

Datasheet & SDS

Biological Description

Specificity
SH2D1A Antibody [C12N16] detects endogenous levels of total SH2D1A protein.

Clone
C12N16

Synonym(s)
SH2 domain-containing protein 1A; Duncan disease SH2-protein; Signaling lymphocytic activation molecule-associated protein (SLAM-associated protein); T-cell signal transduction molecule SAP; SH2D1A; DSHP; SAP

Background
SH2D1A, also known as SAP or SLAM-associated protein, is a small intracellular adaptor protein belonging to the SH2 domain family, encoded by the X-linked SH2D1A gene and predominantly expressed in T cells, NK cells, NKT cells, and B cells. It consists of a single SH2 domain flanked by short N- and C-terminal tails, and features a unique phosphotyrosine-independent binding pocket with key residues including arginine 28, serine 35, and arginine 78 that recognize a three-pronged motif on SLAM family receptors such as SLAM, 2B4, and others. SAP/SH2D1A exhibits high-affinity binding to SLAM family receptors that does not require phosphorylation, distinguishing it from conventional SH2 domains, which depend on phosphotyrosine recognition. This unique interaction relies on a 'three-pronged' motif engaging key SH2 residues, enabling robust adaptor function. The protein displays structural flexibility, with distinct conformational complexes formed upon ligand binding and no long-range contacts detected beyond residue 105. SAP recruits Src family kinases like Fyn via SH3 domain interactions to SLAM receptors and competitively blocks the recruitment of inhibitory phosphatases such as SHP-1 and SHP-2. This leads to activation of downstream MAPK/ERK signaling, calcium flux, and cytokine production including interferon-gamma and TNF-alpha, thereby promoting cytotoxicity, lytic granule polarization in cytotoxic T and NK cells, NKT cell development, T-B cell interactions required for germinal center formation, and restimulation-induced cell death that prevents lymphoproliferation. SAP is crucial for antiviral immunity, especially against Epstein-Barr virus, for humoral immune responses, and for maintaining immune homeostasis. Mutations in SH2D1A, of which about fifty are reported and often truncate the protein or disrupt SH2 binding, abolish these functions and result in X-linked lymphoproliferative disease type 1, also known as Duncan's disease. This disorder is characterized by fatal Epstein-Barr virus-induced mononucleosis, a high risk of lymphoma, hypogammaglobulinemia, and hemophagocytic lymphohistiocytosis due to unchecked B cell proliferation and failed cytotoxic immune responses.

Background

SH2D1A, also known as SAP or SLAM-associated protein, is a small intracellular adaptor protein belonging to the SH2 domain family, encoded by the X-linked SH2D1A gene and predominantly expressed in T cells, NK cells, NKT cells, and B cells. It consists of a single SH2 domain flanked by short N- and C-terminal tails, and features a unique phosphotyrosine-independent binding pocket with key residues including arginine 28, serine 35, and arginine 78 that recognize a three-pronged motif on SLAM family receptors such as SLAM, 2B4, and others. SAP/SH2D1A exhibits high-affinity binding to SLAM family receptors that does not require phosphorylation, distinguishing it from conventional SH2 domains, which depend on phosphotyrosine recognition. This unique interaction relies on a 'three-pronged' motif engaging key SH2 residues, enabling robust adaptor function. The protein displays structural flexibility, with distinct conformational complexes formed upon ligand binding and no long-range contacts detected beyond residue 105. SAP recruits Src family kinases like Fyn via SH3 domain interactions to SLAM receptors and competitively blocks the recruitment of inhibitory phosphatases such as SHP-1 and SHP-2. This leads to activation of downstream MAPK/ERK signaling, calcium flux, and cytokine production including interferon-gamma and TNF-alpha, thereby promoting cytotoxicity, lytic granule polarization in cytotoxic T and NK cells, NKT cell development, T-B cell interactions required for germinal center formation, and restimulation-induced cell death that prevents lymphoproliferation. SAP is crucial for antiviral immunity, especially against Epstein-Barr virus, for humoral immune responses, and for maintaining immune homeostasis. Mutations in SH2D1A, of which about fifty are reported and often truncate the protein or disrupt SH2 binding, abolish these functions and result in X-linked lymphoproliferative disease type 1, also known as Duncan's disease. This disorder is characterized by fatal Epstein-Barr virus-induced mononucleosis, a high risk of lymphoma, hypogammaglobulinemia, and hemophagocytic lymphohistiocytosis due to unchecked B cell proliferation and failed cytotoxic immune responses.

References
https://pubmed.ncbi.nlm.nih.gov/11823424/ https://pubmed.ncbi.nlm.nih.gov/20926771/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%