Recombinant Human LYPD3 Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1226NP
BL-1226NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1226NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human LYPD3 Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1226NP
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Product Overview

Description Recombinant Human Ly6/PLAUR Domain-Containing Protein 3 is produced by our Mammalian expression system and the target gene encoding Leu31-His286 is expressed with a 6His tag at the C-terminus.
Accession O95274
Synonym Ly6/PLAUR Domain-Containing Protein 3; GPI-Anchored Metastasis-Associated Protein C4.4A Homolog; Matrigel-Induced Gene C4 Protein; MIG-C4; LYPD3; C4.4A
Gene Background Ly6/PLAUR domain containing3 (LYPD-3) is a GPI-linked protein. The structure of LYPD-3 is similar to the urokinasetype plasminogen activator receptor (uPAR). LYPD-3 is a 6 -100 kDa molecule with variable cell type-specific N-O-linked glycosylation, mature human LYPD-3 contains two uPAR/Ly6 domains and a Ser/Thr/Pro-rich (STP) region includes a protease sensitive site . The interaction of LYPD-3 with Laminin 1 and 5 on neighboring cells promotes the adhesion, spreading, and migration of tumor cells. LYPD-3 additionally interacts with Galectin-3 and the anterior gradient proteins AG-2 and AG-3. LYPD-3 overexpression in non-small cell lung cancer is predictive of increased mortality.
Molecular Mass 27.89 KDa
Apmol Mass 55-75 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Supports cell migration. May be involved in urothelial cell-matrix interactions. May be involved in tumor progression.
Subcellular Location Cell membrane; Lipid-anchor, GPI-anchor.
Database References
Tissue Specificity Expressed in placenta, skin and urothelium. Found in suprabasal keratinocytes of chronic wounds. Weak expression is found in esophagus and peripheral blood mononuclear cells. Found in the majority of primary and metastatic transitional cell carcinomas (TC

Gene Functions References

  1. While in the healthy liver hepatocytes are C4.4A negative, data show that C4.4A is strongly expressed in hepatocellular carcinoma (HCC) with upregulation at the invasive front and in lung metastasis, indicating that C4.4A apparently contributes to HCC progression. PMID: 29048672
  2. Our results are consistent with previous data in mouse embryogenesis and wound healing. Based on these findings, we conclude that this human TES model provides an excellent surrogate for studies of C4.4A and Haldisin expressions in human stratified epithelia. PMID: 29075641
  3. Expression and crystallographic studies of the D1D2 domains of C4.4A have been reported. PMID: 28777093
  4. LYPD3 has a role in the maintenance of colorectal cancer stem-like cells. PMID: 28238780
  5. Highly expressed C4.4A protein in HER2-positive human breast cancers indicate a good prognosis. PMID: 23918676
  6. overexpression of C4.4A correlates with metastatic potential of gastric cancer and C4.4A could be a novel independent prognostic marker for predicting outcome. PMID: 24935570
  7. expression of the Ly6/uPAR-domain proteins C4.4A and Haldisin in non-invasive and invasive skin lesions PMID: 25414274
  8. Tenascin-C expression was significantly associated with C4.4A expression in clinical esophageal squamous carcinoma samples suggesting that there may be a functional role for the C4.4A to induceTenascin-C in vivo. PMID: 23708783
  9. findings suggest that a tight association between C4.4A and tumor budding may, in part, be due to C4.4A promoting epithelial-mesenchymal transition at the invasive front of colorectal cancer PMID: 22404718
  10. the first explanation for the C4.4A contribution to wound healing and metastasis. PMID: 22431918
  11. data indicate that expression of the C4.4A protein at the invasive front acts as a novel prognostic marker in colorectal cancer, possibly through invasion-related mechanisms PMID: 20825414
  12. hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan PMID: 12592373
  13. High tumour cell C4.4A expression is associated with shorter survival for non-small cell lung cancer patients. PMID: 17706320
  14. Overexpression of C4.4A is associated with invasion and metastasis of esophageal squamous cell carcinoma PMID: 17849475
  15. we consider C4.4A as a candidate diagnostic marker in colorectal cancer, which possibly can be detected in body fluids PMID: 17912244
  16. cleavage of C4.4A by ADAM10 and ADAM17 contributes to tumor progression PMID: 18979631

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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