Recombinant Proteins

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SH3BGRL Human

SH3 Domain Binding Glutamic Acid-Rich Protein Like Human Recombinant

SH3BGRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-114 a.a) and having a molecular mass of 15.3kDa.
SH3BGRL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25553
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

SH3BGRL2 Human

SH3 Domain Binding Glutamic Acid-Rich Protein Like 2 Human Recombinant

SH3BGRL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 130 amino acids (1-107) and having a molecular mass of 14.7 kDa.
SH3BGRL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25632
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

SH3BGRL3 Human

SH3 Domain Binding Glutamic Acid-Rich Protein Like 3 Human Recombinant

SH3BGRL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 116 amino acids (1-93) and having a molecular mass of 12.8 kDa.
SH3BGRL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25720
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

SH3GL2 Human

SH3-domain GRB2-like 2 Human Recombinant

SH3GL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-352 a.a) and having a molecular mass of 42.5kDa.
SH3GL2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25812
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

SH3GLB1 Human

SH3-domain GRB2-like endophilin B1 Human Recombinant

SH3GLB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 373 amino acids (1-365) and having a molecular mass of 41.9 kDa. SH3GLB1 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25916
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

SH3GLB2 Human

SH3-domain GRB2-like endophilin B2 Human Recombinant

SH3GLB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-395a.a.) and having a molecular mass of 46.4 kDa. SH3GLB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26012
Source
E.coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

The SRC Homology 3 (SH3) domain is a small protein domain consisting of approximately 60 amino acid residues. It was initially identified as a conserved sequence in the viral adaptor protein v-Crk. SH3 domains are present in various proteins, including phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src . They are found in proteins involved in signaling pathways that regulate the cytoskeleton, Ras protein, and Src kinase . SH3 domains are classified based on their ability to bind to proline-rich motifs (PRMs) and are found in both eukaryotic and prokaryotic organisms .

Biological Properties

SH3 domains exhibit a characteristic beta-barrel fold consisting of five or six β-strands arranged as two tightly packed anti-parallel β sheets . They are involved in protein-protein interactions and mediate the assembly of specific protein complexes by binding to proline-rich peptides . SH3 domains are expressed in various tissues and are involved in numerous cellular processes, including cell survival, proliferation, differentiation, migration, and polarity .

Biological Functions

The primary biological function of SH3 domains is to facilitate transient protein-protein interactions by selectively interacting with proline-rich motifs . They play a crucial role in immune responses and pathogen recognition by mediating the assembly of protein complexes involved in these processes . SH3 domains are also implicated in the regulation of cytoskeletal dynamics, cell signaling, and cellular communication .

Modes of Action

SH3 domains interact with other molecules and cells through their ability to bind to proline-rich motifs in their binding partners . This interaction is mediated by the hydrophobic pocket of the SH3 domain, which binds to the proline-rich sequence . SH3 domains are involved in downstream signaling cascades by regulating the interactions of proteins involved in cytoplasmic signaling . They also play a role in the regulation of important cellular pathways, such as cell proliferation, migration, and cytoskeletal modifications .

Regulatory Mechanisms

The expression and activity of SH3 domains are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Phosphorylation of tyrosine residues within the SH3 domain can act as a regulatory switch, controlling the binding affinity of the SH3 domain to its interacting partners . This regulation allows SH3 domains to adopt different conformations and interact with various proteins, thereby modulating their activity and function .

Applications

SH3 domains have numerous applications in biomedical research, diagnostic tools, and therapeutic strategies . They are used as models to study protein-protein interactions and the mechanisms of aggregation and specificity of interactions . SH3 domains are also attractive drug targets due to their involvement in various cellular processes, such as migration, invasiveness, and actin reorganization . High-affinity peptides that bind SH3 domains are being developed as candidates for anticancer treatment .

Role in the Life Cycle

SH3 domains play a significant role throughout the life cycle, from development to aging and disease . They are involved in the regulation of cellular processes essential for development, such as cell survival, proliferation, and differentiation . SH3 domains also play a role in aging and disease by regulating the interactions of proteins involved in cellular signaling and communication . Their dysregulation can lead to various diseases, including cancer, leukemia, osteoporosis, Alzheimer’s disease, and infections .

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