Recombinant Human Sh3 And Px Domain-Containing Protein 2A (SH3PXD2A) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-02501P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Sh3 And Px Domain-Containing Protein 2A (SH3PXD2A) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-02501P
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Product Overview

Description Recombinant Human Sh3 And Px Domain-Containing Protein 2A (SH3PXD2A) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q5TCZ1
Target Symbol SH3PXD2A
Synonyms Adapter protein TKS5; Five SH3 domain-containing protein; SH3 and PX domain-containing protein 2A; SH3 multiple domains protein 1; Sh3md1; Sh3pxd2a; SPD2A_HUMAN; TKs5; Tyrosine kinase substrate with five SH3 domains
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence PDPSGKELDTVPAKGRQNEGKSDSLEKIERRVQALNTVNQSKKATPPIPSKPPGGFGKTSGTPAVKMRNGVRQVAVRPQSVFVSP
Expression Range 902-986aa
Protein Length Partial
Mol. Weight 14.0 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide.
Subcellular Location Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.
Protein Families SH3PXD2 family
Database References
Tissue Specificity Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas.

Gene Functions References

  1. Our results suggest that dissociation between XB130 and Tks5 may facilitate lateral cell migration via XB130/Rac1, and vertical cell migration via Tks5/Cdc42. These molecular mechanisms will help our understanding of airway epithelial repair and regeneration. PMID: 27835612
  2. Suggest the importance of Tks adaptor proteins in melanoma growth and metastasis in vivo is likely via functional invadopodia formation. PMID: 27802184
  3. Rheumatoid arthritis T cells abundantly express the podosome scaffolding protein TKS5, which enables them to form tissue-invasive membrane structures. TKS5 overexpression was regulated by the intracellular metabolic environment of RA T cells-specifically, by reduced glycolytic flux that led to deficiencies in ATP and pyruvate. PMID: 28737753
  4. Results show that the interaction between Girdin and Tks5 might be important for Tks5 phosphorylation in HCC cells. PMID: 28390157
  5. This is the first study that identifies a new Rab40b-Tks5- and miR-204-dependent invadopodia transport pathway that regulates MMP2 and MMP9 secretion, and extracellular matrix remodeling during cancer progression. PMID: 27789576
  6. Results suggest that Tks5, similar to XB130, plays a role in cell proliferation and cell survival and that the interaction between XB130 and Tks5 appears to be critical for regulation of Src-mediated cellular homeostasis. PMID: 26446840
  7. TKS5 and MYLK represent two mediators of invasive behavior of cancer cells that are regulated by the ZEB1/miR-200 feedback loop PMID: 26334100
  8. establishes an important role for Tks5 in tumor growth in vivo, and suggests that invadopodia may play broad roles in tumor progression PMID: 25826475
  9. Results show that TKS5 is highly expressed in many cancer types with strong correlation with increased metastatic events and a poorer prognosis suggesting a clinical importance. PMID: 24993883
  10. Inhibiting the function of Tks5 both reduced extracellular matrix degradation in vitro and disrupted motoneuron axons from exiting the spinal cord and extending into the periphery. PMID: 25564649
  11. Tks5 is needed for breast carcinoma cell invadopodium precursor stabilization, where the phox homology (PX) domain of Tks5 interacts with PI(3,4)P2. SHIP2 arrival at the invadopodium precursor coincides with the onset of PI(3,4)P2 accumulation. PMID: 24206842
  12. Src-dependent Tks5 phosphorylation regulates invadopodia-associated invasion in prostate cancer cells. PMID: 24174371
  13. Genes including LEP and SH3PXD2A were differentially expressed (p<0.05 and fold change >1.5) in pre-eclampsia placentas. PMID: 23544093
  14. high Tks5long and low Tks5short expressions in human lung adenocarcinomas correlated with metastatic disease and predicted worse survival of early stage patients PMID: 23873940
  15. Tks5, a master regulator of invadopodia in cancer cells, is crucial for osteoclast fusion downstream of phosphoinositide 3-kinase and Src. PMID: 22584907
  16. Tks5 or cortactin occurred in all grades of tumours and expression of Tks5, but not cortactin, was associated with significantly reduced patient survival among glioma patients PMID: 22249020
  17. Tks4 and Tks5 directly bind to NoxA1. The integrity of the N-terminal PRR of NoxA1 is essential for this direct interaction with the Tks proteins. PMID: 20609497
  18. Results demonstrate that Tks5 plays a central role in the recruitment of AFAP-110, p190RhoGAP, and cortactin to drive podosome formation. PMID: 19540230
  19. Tks5/Fish appears to be required for podosome formation, for degradation of the extracellular matrix, and for invasion of some cancer cells PMID: 15710328
  20. The tandem SH3A and SH3B domains of Tks5 constitute a versatile module for the implementation of isoform-specific protein-protein interactions. PMID: 19464300
  21. Tks proteins selectively support Nox1 and Nox3 (and not Nox2 and Nox4) activity in reconstituted cellular systems and interact with the NoxA1 activator protein through an Src homology 3 domain-mediated interaction PMID: 19755710

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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