Recombinant Human LGALS7 Protein

Beta LifeScience SKU/CAT #: BL-2022NP
BL-2022NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-2022NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human LGALS7 Protein

Beta LifeScience SKU/CAT #: BL-2022NP
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Product Overview

Description Recombinant Human Galectin-7 is produced by our E.coli expression system and the target gene encoding Met1-Phe136 is expressed.
Accession P47929
Synonym Galectin-7; Gal-7; HKL-14; PI7; p53-Induced Gene 1 Protein; LGALS7; PIG1; LGALS7B
Gene Background The Galectin family of proteins, with specificity for Nacetyllactosamine containing glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs).They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide; they can be secreted by one or more as yet unidentified non-classical secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications.
Molecular Mass 15.07 KDa
Apmol Mass 14 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM EDTA, 5% Trehalose, pH 8.0.
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 Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release.
Subcellular Location Cytoplasm. Nucleus. Secreted. Note=May be secreted by a non-classical secretory pathway.
Database References
Tissue Specificity Mainly expressed in stratified squamous epithelium.

Gene Functions References

  1. Increased O-linked N-Acetyl-glucosamine (O-GlcNAc) is responsible for reduced Gal-7 expression in cultured human keratinocytes exposed to high glucose environment. PMID: 28526214
  2. We observed a significantly reduced overall survival for cases with high Gal-7 expression and a better survival for Gal-7 negative cases, when compared to cases with low expression of Gal-7. PMID: 28594391
  3. Data suggest that evaluation of galectin-7 could help guide postsurgical management for non-metastatic clear cell renal cell carcinoma (ccRCC). PMID: 27259255
  4. these findings reveal the existence of a positive self-amplification pathway that regulates intracellular gal-7 expression in breast and ovarian cancer cells. PMID: 29117220
  5. Gal-7 re-expression affects the regulation of molecular networks in cervical cancer that are involved in diverse cancer hallmarks, such as metabolism, growth control, invasion and evasion of apoptosis PMID: 27558259
  6. Measurement of scGal-7 content in tape-stripped samples was useful for the evaluation of the skin barrier function in dry skin conditions such as AD PMID: 27028525
  7. Data indicate that the galectin inhibitor specifically binds galectin-7 (hGal-7), disrupts the formation of homodimers, and inhibits the pro-apoptotic activity of hGal-7 on Jurkat T cells. PMID: 26543238
  8. Galectin-7 regulates keratinocytes proliferation and differentiation through JNK1 pathway. PMID: 26763438
  9. The assessment of a carbohydrate-recognition domain (CRD)-defective mutant form of gal-7 (R7S) showed that the ability of this protein to modulate apoptosis was independent of its CRD activity. PMID: 26168167
  10. our study validates the clinical significance of gal-7 overexpression in ovarian cancer PMID: 25277199
  11. Cytosolic galectin-7 impairs p53 functions and induces chemoresistance in breast cancer cells. PMID: 25367122
  12. Galectin-7 is produced by the premenstrual and menstrual endometrium, where it accumulates in menstrual fluid and likely acts as a paracrine factor to facilitate post-menstrual endometrial re-epithelialization. PMID: 24782449
  13. Understanding how these dendrimeric compounds interact with hGal-7 would help in the design of new tools to investigate the recognition of carbohydrates by lectins. PMID: 25367374
  14. galectin-7 is a potential predictive marker of chemotherapy and/or radiotherapy resistance in patients with oral squamous cell carcinoma PMID: 24515895
  15. galectin-7 may have a role in amyloidogenesis of primary localized cutaneous amyloidosis PMID: 25172508
  16. C/EBPbeta is an important mediator of galectin-7 gene activation in breast cancer cells PMID: 24789216
  17. Galectin-7 is produced by endometrial epithelium. It is elevated in the endometrium of women with history of miscarriage. We suggest that galectin-7 facilitates adhesion of embryo to endometrium. Elevated galectin-7 may result in abnormal adhesion. PMID: 24522232
  18. galectin-7 may play important roles in downregulating the functions of T lymphocytes after UVB irradiation PMID: 24134186
  19. galectin-7 has a tumor suppressive function, and that the gene is epigenetically modified by DNA methylation and significantly down-regulated in gastric cancer. PMID: 23985992
  20. Suggest that the differences in galectin-7 expression and subcellular and extracellular distribution may be crucially involved in the pathogenic process of hypertrophic scars. PMID: 23493985
  21. galectin-7 could be part of a common pathway used by mutant p53 to promote cancer progression PMID: 23967302
  22. The results indicate that lactose binding to human Gal-7 induces long-range effects (minor conformational shifts and changes in structural dynamics) throughout the protein that result in stabilization of the dimer state, with evidence for positive cooperativity. PMID: 23376190
  23. High GAL-7 expression is associated with epithelial ovarian cancer. PMID: 23564797
  24. Knocking down galectin-7 or S100A9 enhanced tumor cell invasion. PMID: 22864818
  25. Because residual cholesteatoma matrix is considered to be one of the main causes of cholesteatoma recurrence, staining with galectin-7 at the time of operation would be a promising way to facilitate complete removal of the residue PMID: 22377647
  26. Extracellular superoxide dismutase plays a role not only as a reactive oxygen species scavenger, but also as a pro-apoptotic factor via COX-2/galectin-7 pathways in the epidermis. PMID: 22251572
  27. high resolution crystal structure of Gal-7 at 1.4 A (a dimer) and its 1.7 A structure in complex with an inhibitor, a sulfur-containing 2-O-benzylphosphate galactoside, a possible antineoplastic agent PMID: 22059385
  28. Data suggest that the binding of Galectin 7 to Bcl-2 may constitute a new target for enhancing the intrinsic apoptosis pathway. PMID: 21289092
  29. Galectin-7 modulates the length of the primary cilia and wound repair in polarized kidney epithelial cells. PMID: 21677144
  30. Data show that high levels of galectin-7 expression in breast cancer cells drastically increased their ability to metastasize to lungs and bones, and were restricted to high-grade breast carcinomas. PMID: 20382700
  31. Proteomics analysis revealed that galectin-7 was highly expressed in esophageal squamous cell carcinoma and could be used as a potential biomarker. PMID: 20546628
  32. Data show that Galectine-7 gene was 8 times up-regulated in bronchial epithelial cells from asthmatic children after RSV infection in vitro and overexpressed in bronchial epithelial cells in asthma in vivo. PMID: 17044979
  33. galectin-7 increases the expression of MMP-9 through the p38 MAPK signaling pathway PMID: 19885589
  34. GAL7 is a negative growth regulator for human neuroblastoma cells. PMID: 13679866
  35. High levels of galectin 7 expression were associated with rapid recurrence rates in hypopharyngeal cancer PMID: 16788763
  36. there was no significant difference in Galectin 7 expression in thyroid tissue in thyroid cancer cases compared to non-cancer cases PMID: 18418527
  37. Gal-7 influence on differentiation in vivo, without evidence for a role in dissemination in head and neck squamous and basal cell carcinomas PMID: 19012243
  38. abnormal expression of galectin-7 in lymphoma cells is not dependent on p53, but is rather associated with DNA hypomethylation. PMID: 19596268


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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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