Recombinant Human Laminin Subunit Gamma-2 (LAMC2) Protein (His-GST&Myc)

Beta LifeScience SKU/CAT #: BLC-11032P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Laminin Subunit Gamma-2 (LAMC2) Protein (His-GST&Myc)

Beta LifeScience SKU/CAT #: BLC-11032P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Laminin Subunit Gamma-2 (LAMC2) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q13753
Target Symbol LAMC2
Synonyms 3918; B2T; BM600; Cell-scattering factor 140 kDa subunit; CSF 140 kDa subunit; CSF; EBR2; EBR2A; Epiligrin subunit gamma; Kalinin subunit gamma; Kalinin/nicein/epiligrin 100 kDa subunit; Ladsin 140 kDa subunit; LAMB2T; LAMC2; LAMC2_HUMAN; Laminin 5 gamma 2 subunit; Laminin B2t chain; Laminin gamma 2; laminin gamma 2 chain; Laminin subunit gamma-2; Laminin-5 subunit gamma; LAMNB2; Large adhesive scatter factor 140 kDa subunit; MGC138491; MGC141938; Nicein subunit gamma; NICEIN-100KDA
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His-GST&C-Myc
Target Protein Sequence NCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQPCQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPMGSEPVGCRSD
Expression Range 417-588aa
Protein Length Partial
Mol. Weight 53.3 kDa
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 Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.
Subcellular Location Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
Database References
Associated Diseases Epidermolysis bullosa, junctional, Herlitz type (H-JEB)
Tissue Specificity The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.

Gene Functions References

  1. It regulates tumor development of tongue squamous cell carcinoma together with LINC00511 and miR-765. PMID: 29315846
  2. Laminin 332 was expressed specifically within papillary thyroid carcinoma (PTC) tissue. The frequency of laminin 332 gamma2 chain expression was significantly correlated with cervical lymph node metastasis. Invasiveness increased as the expression of laminin 332 gamma2 increased in the tested PTC cell lines. PMID: 28238469
  3. Study found that high expression of LAMC2 was significantly associated with shorter disease-free survival in GC and, that expression of LAMC2 was significantly upregulated when PCDH8 was overexpressed. PMID: 29325230
  4. The results of this study highlight the value of LAMC2 as a marker of cancer invasion. LAMC2-positive foci in leukoplakia suggest an imminent risk of cancer. PMID: 27529842
  5. Results indicate that LAMC2-Dox mice expressing the human protein are unable to sustain structuring of a proper basement membrane (BM) at the interface between ameloblasts and maturing enamel. This failure may be related to the atypical composition of the BM in the maturation stage and reaffirms that the atypical BM is essential for enamel maturation. PMID: 26956061
  6. The data presented provide a novel insight into how CDX2 is implicated in the transcriptional regulation of LAMC2 in intestinal epithelial cells, a function that is impaired during mucosal inflammation where a high level of TNF-alpha is present. PMID: 27333824
  7. our results strongly suggest that laminin g2 may be a potential prognostic biomarker and therapeutic target in colorectal cancer. PMID: 28653882
  8. Laminin expression depends on Ecad loss and allows Ecad-defective gastric cancer cells to survive and invade. PMID: 26246502
  9. findings strongly indicate that Ln-gamma2 is an attractive biomarker for detecting early stages of UC and for monitoring recurrence PMID: 26450632
  10. Data suggest that LAMC2 promotes metastasis in lung adenocarcinoma via EMT and may be a potential therapeutic target. PMID: 25591736
  11. The positive expression of laminingamma2 and the tumor differentiation were independent risk factors influencing the prognosis of EHCC patients. PMID: 25773857
  12. LAMC2 is a novel non-small cell lung cancer prognostic factor. PMID: 26180921
  13. Diagnostic value of p40 and LN332 in metaplastic spindle cell carcinoma of the breast was found to be less than that of routinely used markers (p63 and cytokeratins). LN332 showed staining in a significant proportion of phyllodes tumours and sarcomas. PMID: 25795733
  14. The elevated expression of LAMC2 on cancer cells appears to drive tumorigenesis through its interactions with several cell-surface receptors PMID: 24976367
  15. Molecular expression of MMP-7, laminin c2 or EGFR, and their combinations, may be associated with gastric cancer tumor aggressiveness PMID: 24048760
  16. Through an unbiased genetic approach involving a combination of QTL mapping and positional cloning, we demonstrate that Col17a1 is a strong genetic modifier of the non-Herlitz JEB that develops in Lamc2(jeb) mice PMID: 24550734
  17. LAMC2 is expressed at a higher level in ectopic endometrium (Ec) from women with endometriosis compared with eutopic endometrium (Eu) from women with endometriosis. PMID: 24070183
  18. The active site of gamma2pf to the N-terminal epidermal growth factor-like repeat. PMID: 24238220
  19. LAMC2 is a promising new putative pancreatic cancer biomarker identified by proteomic analysis of pancreatic adenocarcinoma tissues. PMID: 23798558
  20. LAMC2 may be a potential therapeutic target for the treatment of anaplastic thyroid carcinoma. PMID: 24170107
  21. Both stromal and cytoplasmic laminin gamma2 expressions correlated with lymph node metastasis PMID: 24124977
  22. Lamininn-5 gamma 2 EPHA2 signaling contributed to tumor growth and vasculogenic mimicry of gallbladder carcinomas. PMID: 23588386
  23. both laminin- 5gamma2 chain staining and tumor budding are associated with tumor cell invasiveness and are independent predictors of mortality in lung SqCC patients. PMID: 23124251
  24. Expression of Ln-5gamma2 in the invasive front of lip squamous cell carcinoma and its correlation with tumor progression suggest it mediates the acquisition of the migrating and invading epithelial cell phenotype. PMID: 22917688
  25. In colorectal cancer progression, vascular endothelial growth factor overexpression seems to play a role in the tumor center, whereas Laminin5gamma2-positivity combined with Raf-1 kinase inhibitor protein loss is associated with tumor invasion at the front. PMID: 21664646
  26. Data suggest that an anti-Wnt5a antibody was capable of suppressing Wnt5a-dependent internalization of Fz2 receptor, resulting in the prevention of metastasis of gastric cancer cells by inhibiting the activation of Rac1 and the expression of laminin gamma2. PMID: 22101459
  27. Compared with conventional carcinomas, serrated adenocarcinomas showed significantly increased cytoplasmic expression of laminin-5gamma2 at the invasive front that was particularly pronounced in the tumor buds. PMID: 22209340
  28. Cytoplasmic laminin-5 expression should not be used as a criterion of malignancy and is not useful in distinguishing pseudocarcinomatous hyperplasia from microinvasive and well-differentiated SCC. PMID: 21955313
  29. Immunohistochemical analysis of laminin 5-gamma2 chain expression for differentiation of basal cell carcinoma from trichoblastoma. PMID: 21771037
  30. The infiltrative invasion of GI-type ovarian mucinous neoplasms may be promoted by cytoplasmic and/or stromal expression of laminin gamma 2 chain. PMID: 21042753
  31. Increased expression of laminin5-[gamma]2 is associated with bronchioloalveolar carcinoma. PMID: 20631633
  32. These findings imply that the gamma2 monomer is induced in human cancers by inflammatory and stromal cytokines and promotes their invasive growth in vivo. PMID: 20143393
  33. Results show the uncoupled induction of laminin-332 chains in Smad4-negative cells is followed by the release of gamma2 into the medium, either in a monomeric form or in complexes with unknown proteins. Soluble gamma2 is assoc'd with inc'd cell migration. PMID: 20307265
  34. These results show that LN-332, known to have some beneficial effect on beta cells in vitro, is produced and secreted by endocrine islet cells and is up-regulated by stressing conditions. PMID: 19667121
  35. cytoplasmic expression represents high invasive potential of pancreatic ductal adenocarcinoma and is correlated with distant metastasis and poorer prognosis PMID: 11920553
  36. laminin-gamma2 is frequently overexpressed in HNSCCs and derivative cell lines PMID: 11992550
  37. level of circulating LN gamma2 NH(2)-terminal fragment (G2F) is a new, prognostic, tumor-characterizing marker for estimating the invasiveness and malignancy of epithelial carcinomas PMID: 12517801
  38. Thus the synergistic activation of the LAMC2 gene is mediated via different cis-elements and results in an overproduction of the laminin gamma 2 chain relative to the other laminin-5 constituent chains. PMID: 12519076
  39. Laminin-5 gamma2 chain expression may contribute to formation of budding tumor cells at the invasive front, and immunostaining of this adhesion molecule may be useful in identifying high-risk patients for locoregional failure in T1 colorectal carcinomas. PMID: 12643602
  40. epidermis of the Lamc2-/- mice revealed induced apoptosis in the basal cells of the blistered skin PMID: 14632187
  41. Laminin gamma 2 chain exhibits aberrant expression in a stepwise manner through different aggressive stages of tumor progression. PMID: 15105812
  42. In squamous cell carcinoma of the tongue and colorectal carcinoma, laminin 5 gamma2 chain is important in the invasiveness of cancer cells. PMID: 15363037
  43. Data show that the expression of laminin gamma2 chain and collagen type XVII is altered in endometrial adenocarcinomas. PMID: 15609083
  44. up-regulation of Ang2, MMP-2, MT1-MMP, and LN 5 gamma 2 is associated with the invasiveness displayed by human gliomas PMID: 15743799
  45. Ln-5 gamma2 chain regulates the secretion of the alpha3 and beta3 subunits. More importantly, suppression of Ln-5 results in a phenotype that is representative of invasive tumor cells PMID: 15963983
  46. This study suggests that coexpression of LN-5 gamma2 and EGFR is closely related to the progression and poor prognosis of esophageal SCC. PMID: 16103736
  47. Ln-5 and TGF-beta1 cooperatively induce epithelial to mesenchymal transition in hepatocellular carcinoma PMID: 16285938
  48. Our results suggest that PAI-1 is a novel potential marker of initial invasion in oral SCC, and that the coordinated expression of PAI-1 with uPAR and lam-gamma2 sustain the features of the early invasive cancer cells. PMID: 16395714
  49. findings suggest that mesenchymal cells contribute to the promotion of tumour cell migration as well as vessel formation in oral squamous cell carcinoma by providing and organising promigratory Ln-5 fragments PMID: 17390227
  50. Overexpression of Laminin-5 gamma2 is associated with oral squamous cell carcinomas PMID: 17786338

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed