Recombinant Human Galectin-7 (LGALS7) Protein (His)

Name: Recombinant Human Galectin-7 (LGALS7) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08334P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Galectin-7 (LGALS7) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P47929
Target Symbol	LGALS7
Synonyms	Gal-7; GAL7; Galectin 7B; Galectin-7; HKL-14; Human keratinocyte lectin 14 ; Keratinocyte lectin 14; Lectin galactoside binding soluble 7; Lectin; galactoside binding; soluble; 7B; LEG7_HUMAN; LGALS7; LGALS7A; LGALS7B; P53 induced protein 1; p53-induced gene 1 protein; Pi7; PIG1; TP53I1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSVRIF
Expression Range	2-136aa
Protein Length	Full Length of Mature Protein
Mol. Weight	18.9kDa
Research Area	Neuroscience
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.
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	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	HGNC: 6568 OMIM: 600615 KEGG: hsa:3963 STRING: 9606.ENSP00000367891 UniGene: PMID: 28526214 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 Data suggest that evaluation of galectin-7 could help guide postsurgical management for non-metastatic clear cell renal cell carcinoma (ccRCC). PMID: 27259255 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 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 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 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 Galectin-7 regulates keratinocytes proliferation and differentiation through JNK1 pathway. PMID: 26763438 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 our study validates the clinical significance of gal-7 overexpression in ovarian cancer PMID: 25277199 Cytosolic galectin-7 impairs p53 functions and induces chemoresistance in breast cancer cells. PMID: 25367122 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 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 galectin-7 is a potential predictive marker of chemotherapy and/or radiotherapy resistance in patients with oral squamous cell carcinoma PMID: 24515895 galectin-7 may have a role in amyloidogenesis of primary localized cutaneous amyloidosis PMID: 25172508 C/EBPbeta is an important mediator of galectin-7 gene activation in breast cancer cells PMID: 24789216 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 galectin-7 may play important roles in downregulating the functions of T lymphocytes after UVB irradiation PMID: 24134186 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 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 galectin-7 could be part of a common pathway used by mutant p53 to promote cancer progression PMID: 23967302 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 High GAL-7 expression is associated with epithelial ovarian cancer. PMID: 23564797 Knocking down galectin-7 or S100A9 enhanced tumor cell invasion. PMID: 22864818 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 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 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 Data suggest that the binding of Galectin 7 to Bcl-2 may constitute a new target for enhancing the intrinsic apoptosis pathway. PMID: 21289092 Galectin-7 modulates the length of the primary cilia and wound repair in polarized kidney epithelial cells. PMID: 21677144 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 Proteomics analysis revealed that galectin-7 was highly expressed in esophageal squamous cell carcinoma and could be used as a potential biomarker. PMID: 20546628 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 galectin-7 increases the expression of MMP-9 through the p38 MAPK signaling pathway PMID: 19885589 GAL7 is a negative growth regulator for human neuroblastoma cells. PMID: 13679866 High levels of galectin 7 expression were associated with rapid recurrence rates in hypopharyngeal cancer PMID: 16788763 there was no significant difference in Galectin 7 expression in thyroid tissue in thyroid cancer cases compared to non-cancer cases PMID: 18418527 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 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.